Magnesium in PDB 5hat: Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Enzymatic activity of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
All present enzymatic activity of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound):
4.1.1.39;
Protein crystallography data
The structure of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound), PDB code: 5hat
was solved by
M.A.Arbing,
J.G.Leong,
D.Cascio,
V.A.Varaljay,
S.Satagopan,
J.A.North,
F.R.Tabita,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.00
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
76.140,
111.030,
167.260,
90.03,
101.69,
105.05
|
R / Rfree (%)
|
21.3 /
24.9
|
Magnesium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Magnesium atom in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
(pdb code 5hat). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 12 binding sites of Magnesium where determined in the
Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound), PDB code: 5hat:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Magnesium binding site 1 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 1 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg501
b:37.2
occ:1.00
|
HO3
|
A:CAP500
|
1.4
|
37.8
|
1.0
|
OD1
|
A:ASP194
|
2.0
|
38.1
|
1.0
|
O2
|
A:CAP500
|
2.0
|
45.3
|
1.0
|
O6
|
A:CAP500
|
2.1
|
36.3
|
1.0
|
OQ2
|
A:KCX192
|
2.1
|
36.0
|
1.0
|
OE1
|
A:GLU195
|
2.2
|
41.9
|
1.0
|
O3
|
A:CAP500
|
2.2
|
38.9
|
1.0
|
HO2
|
A:CAP500
|
2.6
|
44.8
|
1.0
|
C2
|
A:CAP500
|
2.7
|
39.8
|
1.0
|
C
|
A:CAP500
|
2.7
|
35.4
|
1.0
|
H
|
A:GLU195
|
2.9
|
40.8
|
1.0
|
C3
|
A:CAP500
|
2.9
|
40.0
|
1.0
|
HZ3
|
A:LYS167
|
3.0
|
46.1
|
1.0
|
HD21
|
B:ASN112
|
3.0
|
38.8
|
1.0
|
CX
|
A:KCX192
|
3.1
|
36.5
|
1.0
|
CG
|
A:ASP194
|
3.2
|
42.8
|
1.0
|
CD
|
A:GLU195
|
3.2
|
51.9
|
1.0
|
HG21
|
A:ILE165
|
3.3
|
34.7
|
1.0
|
HE2
|
A:HIS288
|
3.4
|
35.5
|
1.0
|
OQ1
|
A:KCX192
|
3.4
|
39.0
|
1.0
|
H3
|
A:CAP500
|
3.4
|
38.3
|
1.0
|
HZ2
|
A:LYS169
|
3.4
|
50.8
|
1.0
|
HA
|
A:ASP194
|
3.5
|
36.3
|
1.0
|
HZ3
|
A:LYS169
|
3.5
|
52.5
|
1.0
|
HZ1
|
A:LYS169
|
3.6
|
51.7
|
1.0
|
NZ
|
A:LYS169
|
3.7
|
51.9
|
1.0
|
HD22
|
B:ASN112
|
3.7
|
39.5
|
1.0
|
ND2
|
B:ASN112
|
3.7
|
38.8
|
1.0
|
OE2
|
A:GLU195
|
3.7
|
39.5
|
1.0
|
OD2
|
A:ASP194
|
3.8
|
47.8
|
1.0
|
NZ
|
A:LYS167
|
3.8
|
47.0
|
1.0
|
HZ2
|
A:LYS167
|
3.9
|
46.9
|
1.0
|
N
|
A:GLU195
|
3.9
|
39.2
|
1.0
|
O7
|
A:CAP500
|
3.9
|
33.5
|
1.0
|
NE2
|
A:HIS288
|
4.1
|
35.5
|
1.0
|
C1
|
A:CAP500
|
4.1
|
38.2
|
1.0
|
HB3
|
A:GLU195
|
4.1
|
41.0
|
1.0
|
HZ1
|
A:LYS167
|
4.1
|
47.2
|
1.0
|
HG12
|
A:ILE165
|
4.2
|
35.4
|
1.0
|
CA
|
A:ASP194
|
4.2
|
35.8
|
1.0
|
C4
|
A:CAP500
|
4.3
|
45.7
|
1.0
|
CB
|
A:ASP194
|
4.3
|
36.2
|
1.0
|
CG2
|
A:ILE165
|
4.3
|
35.4
|
1.0
|
NZ
|
A:KCX192
|
4.3
|
33.8
|
1.0
|
H4
|
A:CAP500
|
4.4
|
44.5
|
1.0
|
CG
|
A:GLU195
|
4.5
|
42.1
|
1.0
|
H12
|
A:CAP500
|
4.5
|
37.0
|
1.0
|
O1
|
A:CAP500
|
4.5
|
33.0
|
1.0
|
HD3
|
A:PRO196
|
4.5
|
43.5
|
1.0
|
HE1
|
A:HIS288
|
4.5
|
35.7
|
1.0
|
C
|
A:ASP194
|
4.6
|
40.8
|
1.0
|
HG23
|
A:ILE165
|
4.6
|
33.9
|
1.0
|
H52
|
A:CAP500
|
4.6
|
42.4
|
1.0
|
CE1
|
A:HIS288
|
4.7
|
35.1
|
1.0
|
CB
|
A:GLU195
|
4.7
|
39.9
|
1.0
|
H11
|
A:CAP500
|
4.7
|
38.5
|
1.0
|
HG22
|
A:ILE165
|
4.7
|
35.8
|
1.0
|
HG3
|
A:LYS169
|
4.8
|
49.9
|
1.0
|
O
|
B:HOH685
|
4.9
|
42.2
|
1.0
|
HE2
|
A:LYS167
|
4.9
|
46.7
|
1.0
|
C5
|
A:CAP500
|
4.9
|
42.2
|
1.0
|
CA
|
A:GLU195
|
4.9
|
38.8
|
1.0
|
HB3
|
A:ASP194
|
4.9
|
36.0
|
1.0
|
H51
|
A:CAP500
|
4.9
|
41.8
|
1.0
|
CG
|
B:ASN112
|
5.0
|
41.5
|
1.0
|
HB2
|
A:ASP194
|
5.0
|
36.8
|
1.0
|
|
Magnesium binding site 2 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 2 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg501
b:33.3
occ:1.00
|
HO3
|
B:CAP500
|
1.5
|
38.0
|
1.0
|
OD1
|
B:ASP194
|
1.9
|
36.6
|
1.0
|
OE1
|
B:GLU195
|
2.0
|
30.9
|
1.0
|
OQ1
|
B:KCX192
|
2.0
|
34.8
|
1.0
|
O6
|
B:CAP500
|
2.2
|
44.4
|
1.0
|
O2
|
B:CAP500
|
2.2
|
42.0
|
1.0
|
O3
|
B:CAP500
|
2.3
|
37.9
|
1.0
|
HO2
|
B:CAP500
|
2.7
|
42.7
|
1.0
|
H
|
B:GLU195
|
2.7
|
34.7
|
1.0
|
C2
|
B:CAP500
|
2.8
|
38.1
|
1.0
|
C
|
B:CAP500
|
2.9
|
40.9
|
1.0
|
HD21
|
A:ASN112
|
3.0
|
44.9
|
1.0
|
CX
|
B:KCX192
|
3.1
|
35.0
|
1.0
|
CD
|
B:GLU195
|
3.1
|
51.0
|
1.0
|
C3
|
B:CAP500
|
3.1
|
31.9
|
1.0
|
CG
|
B:ASP194
|
3.1
|
41.0
|
1.0
|
HZ3
|
B:LYS167
|
3.1
|
42.4
|
1.0
|
HG21
|
B:ILE165
|
3.3
|
34.8
|
1.0
|
OQ2
|
B:KCX192
|
3.4
|
35.3
|
1.0
|
HZ2
|
B:LYS169
|
3.4
|
45.6
|
1.0
|
HA
|
B:ASP194
|
3.4
|
32.8
|
1.0
|
H3
|
B:CAP500
|
3.5
|
32.1
|
1.0
|
HZ3
|
B:LYS169
|
3.5
|
45.2
|
1.0
|
OE2
|
B:GLU195
|
3.6
|
53.8
|
1.0
|
HZ1
|
B:LYS169
|
3.7
|
44.6
|
1.0
|
N
|
B:GLU195
|
3.7
|
34.6
|
1.0
|
ND2
|
A:ASN112
|
3.7
|
44.0
|
1.0
|
HD22
|
A:ASN112
|
3.7
|
44.5
|
1.0
|
NZ
|
B:LYS169
|
3.7
|
45.0
|
1.0
|
OD2
|
B:ASP194
|
3.8
|
46.8
|
1.0
|
HB3
|
B:GLU195
|
3.9
|
35.5
|
1.0
|
NZ
|
B:LYS167
|
4.0
|
43.1
|
1.0
|
HZ2
|
B:LYS167
|
4.0
|
43.3
|
1.0
|
NE2
|
B:HIS288
|
4.0
|
40.4
|
1.0
|
O7
|
B:CAP500
|
4.1
|
36.7
|
1.0
|
CA
|
B:ASP194
|
4.1
|
32.3
|
1.0
|
CB
|
B:ASP194
|
4.2
|
33.4
|
1.0
|
HG12
|
B:ILE165
|
4.3
|
36.4
|
1.0
|
C1
|
B:CAP500
|
4.3
|
37.8
|
1.0
|
CG
|
B:GLU195
|
4.3
|
42.2
|
1.0
|
HZ1
|
B:LYS167
|
4.3
|
42.8
|
1.0
|
NZ
|
B:KCX192
|
4.3
|
34.8
|
1.0
|
HD3
|
B:PRO196
|
4.3
|
42.0
|
1.0
|
CG2
|
B:ILE165
|
4.4
|
34.8
|
1.0
|
C4
|
B:CAP500
|
4.4
|
37.2
|
1.0
|
C
|
B:ASP194
|
4.4
|
36.8
|
1.0
|
CB
|
B:GLU195
|
4.4
|
35.5
|
1.0
|
HE1
|
B:HIS288
|
4.5
|
39.6
|
1.0
|
H4
|
B:CAP500
|
4.5
|
39.4
|
1.0
|
CE1
|
B:HIS288
|
4.6
|
39.5
|
1.0
|
H12
|
B:CAP500
|
4.7
|
37.2
|
1.0
|
O1
|
B:CAP500
|
4.7
|
42.6
|
1.0
|
CA
|
B:GLU195
|
4.7
|
34.2
|
1.0
|
HG22
|
B:ILE165
|
4.7
|
35.1
|
1.0
|
H52
|
B:CAP500
|
4.7
|
39.3
|
1.0
|
HG3
|
B:LYS169
|
4.8
|
42.6
|
1.0
|
HG23
|
B:ILE165
|
4.8
|
34.2
|
1.0
|
HB3
|
B:ASP194
|
4.8
|
33.0
|
1.0
|
HG3
|
B:GLU195
|
4.9
|
42.2
|
1.0
|
HD13
|
B:ILE165
|
4.9
|
34.0
|
1.0
|
H11
|
B:CAP500
|
4.9
|
37.3
|
1.0
|
HB2
|
B:ASP194
|
4.9
|
33.5
|
1.0
|
CD2
|
B:HIS288
|
4.9
|
41.2
|
1.0
|
O
|
B:HOH661
|
4.9
|
38.1
|
1.0
|
CG
|
A:ASN112
|
5.0
|
47.5
|
1.0
|
C5
|
B:CAP500
|
5.0
|
39.2
|
1.0
|
HG2
|
B:GLU195
|
5.0
|
42.8
|
1.0
|
|
Magnesium binding site 3 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 3 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg501
b:40.9
occ:1.00
|
HO3
|
C:CAP500
|
1.4
|
39.7
|
1.0
|
OE1
|
C:GLU195
|
1.9
|
37.7
|
1.0
|
OQ1
|
C:KCX192
|
1.9
|
34.5
|
1.0
|
OD1
|
C:ASP194
|
2.0
|
39.4
|
1.0
|
O3
|
C:CAP500
|
2.3
|
41.0
|
1.0
|
O2
|
C:CAP500
|
2.3
|
45.1
|
1.0
|
O6
|
C:CAP500
|
2.3
|
41.6
|
1.0
|
H
|
C:GLU195
|
2.7
|
37.8
|
1.0
|
HO2
|
C:CAP500
|
2.7
|
45.1
|
1.0
|
C2
|
C:CAP500
|
2.9
|
44.9
|
1.0
|
C
|
C:CAP500
|
3.0
|
43.1
|
1.0
|
CX
|
C:KCX192
|
3.0
|
35.6
|
1.0
|
HD21
|
D:ASN112
|
3.0
|
47.1
|
1.0
|
CD
|
C:GLU195
|
3.0
|
57.8
|
1.0
|
C3
|
C:CAP500
|
3.1
|
42.1
|
1.0
|
CG
|
C:ASP194
|
3.1
|
40.9
|
1.0
|
HZ3
|
C:LYS167
|
3.2
|
41.9
|
1.0
|
HE2
|
C:HIS288
|
3.3
|
42.7
|
1.0
|
OQ2
|
C:KCX192
|
3.3
|
37.9
|
1.0
|
HG21
|
C:ILE165
|
3.3
|
39.2
|
1.0
|
HA
|
C:ASP194
|
3.4
|
33.0
|
1.0
|
HZ2
|
C:LYS169
|
3.4
|
45.4
|
1.0
|
H3
|
C:CAP500
|
3.5
|
42.0
|
1.0
|
OE2
|
C:GLU195
|
3.6
|
43.7
|
1.0
|
HZ3
|
C:LYS169
|
3.6
|
45.5
|
1.0
|
N
|
C:GLU195
|
3.6
|
36.8
|
1.0
|
HZ1
|
C:LYS169
|
3.7
|
46.2
|
1.0
|
ND2
|
D:ASN112
|
3.8
|
47.9
|
1.0
|
NZ
|
C:LYS169
|
3.8
|
45.5
|
1.0
|
OD2
|
C:ASP194
|
3.8
|
42.7
|
1.0
|
HD22
|
D:ASN112
|
3.8
|
48.0
|
1.0
|
HB3
|
C:GLU195
|
3.8
|
38.1
|
1.0
|
NE2
|
C:HIS288
|
3.9
|
40.9
|
1.0
|
NZ
|
C:LYS167
|
4.1
|
41.8
|
1.0
|
CA
|
C:ASP194
|
4.1
|
32.5
|
1.0
|
HZ2
|
C:LYS167
|
4.1
|
40.3
|
1.0
|
O7
|
C:CAP500
|
4.2
|
47.0
|
1.0
|
CG
|
C:GLU195
|
4.2
|
53.3
|
1.0
|
CB
|
C:ASP194
|
4.2
|
34.0
|
1.0
|
NZ
|
C:KCX192
|
4.2
|
34.4
|
1.0
|
HG12
|
C:ILE165
|
4.3
|
39.1
|
1.0
|
HD3
|
C:PRO196
|
4.3
|
41.2
|
1.0
|
CB
|
C:GLU195
|
4.4
|
38.1
|
1.0
|
C1
|
C:CAP500
|
4.4
|
44.8
|
1.0
|
C
|
C:ASP194
|
4.4
|
39.6
|
1.0
|
HE1
|
C:HIS288
|
4.4
|
39.1
|
1.0
|
HZ1
|
C:LYS167
|
4.4
|
41.7
|
1.0
|
C4
|
C:CAP500
|
4.4
|
45.9
|
1.0
|
CG2
|
C:ILE165
|
4.4
|
38.6
|
1.0
|
CE1
|
C:HIS288
|
4.5
|
39.7
|
1.0
|
H4
|
C:CAP500
|
4.6
|
46.5
|
1.0
|
CA
|
C:GLU195
|
4.6
|
36.4
|
1.0
|
H52
|
C:CAP500
|
4.7
|
40.4
|
1.0
|
H11
|
C:CAP500
|
4.7
|
43.5
|
1.0
|
HG22
|
C:ILE165
|
4.7
|
40.0
|
1.0
|
O1
|
C:CAP500
|
4.8
|
47.0
|
1.0
|
HG3
|
C:GLU195
|
4.8
|
53.4
|
1.0
|
CD2
|
C:HIS288
|
4.8
|
40.9
|
1.0
|
HG3
|
C:LYS169
|
4.8
|
53.6
|
1.0
|
HB3
|
C:ASP194
|
4.8
|
33.2
|
1.0
|
HG23
|
C:ILE165
|
4.8
|
38.1
|
1.0
|
HG2
|
C:GLU195
|
4.9
|
53.3
|
1.0
|
HD13
|
C:ILE165
|
4.9
|
45.0
|
1.0
|
C5
|
C:CAP500
|
4.9
|
42.0
|
1.0
|
HB2
|
C:ASP194
|
4.9
|
33.7
|
1.0
|
CG
|
D:ASN112
|
5.0
|
55.7
|
1.0
|
H51
|
C:CAP500
|
5.0
|
41.7
|
1.0
|
H12
|
C:CAP500
|
5.0
|
45.3
|
1.0
|
|
Magnesium binding site 4 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 4 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg501
b:44.2
occ:1.00
|
HO3
|
D:CAP500
|
1.5
|
35.6
|
1.0
|
OQ2
|
D:KCX192
|
1.9
|
31.2
|
1.0
|
OD1
|
D:ASP194
|
1.9
|
43.5
|
1.0
|
OE1
|
D:GLU195
|
1.9
|
29.9
|
1.0
|
O7
|
D:CAP500
|
2.2
|
33.3
|
1.0
|
O3
|
D:CAP500
|
2.2
|
36.6
|
1.0
|
O2
|
D:CAP500
|
2.3
|
34.7
|
1.0
|
H
|
D:GLU195
|
2.7
|
32.0
|
1.0
|
HO2
|
D:CAP500
|
2.7
|
34.7
|
1.0
|
C
|
D:CAP500
|
2.9
|
34.6
|
1.0
|
C2
|
D:CAP500
|
2.9
|
36.4
|
1.0
|
HD21
|
C:ASN112
|
3.0
|
31.9
|
1.0
|
CX
|
D:KCX192
|
3.0
|
34.3
|
1.0
|
CD
|
D:GLU195
|
3.0
|
49.6
|
1.0
|
C3
|
D:CAP500
|
3.1
|
38.1
|
1.0
|
CG
|
D:ASP194
|
3.1
|
42.4
|
1.0
|
HZ3
|
D:LYS167
|
3.2
|
40.6
|
1.0
|
HE2
|
D:HIS288
|
3.2
|
40.9
|
1.0
|
OQ1
|
D:KCX192
|
3.3
|
34.1
|
1.0
|
HG21
|
D:ILE165
|
3.3
|
42.2
|
1.0
|
HZ2
|
D:LYS169
|
3.4
|
43.4
|
1.0
|
HA
|
D:ASP194
|
3.4
|
35.0
|
1.0
|
H3
|
D:CAP500
|
3.6
|
37.4
|
1.0
|
OE2
|
D:GLU195
|
3.6
|
45.6
|
1.0
|
HZ3
|
D:LYS169
|
3.6
|
42.9
|
1.0
|
N
|
D:GLU195
|
3.7
|
32.8
|
1.0
|
HZ1
|
D:LYS169
|
3.7
|
44.3
|
1.0
|
ND2
|
C:ASN112
|
3.8
|
32.0
|
1.0
|
NZ
|
D:LYS169
|
3.8
|
43.6
|
1.0
|
HD22
|
C:ASN112
|
3.8
|
31.8
|
1.0
|
OD2
|
D:ASP194
|
3.8
|
39.7
|
1.0
|
HB3
|
D:GLU195
|
3.9
|
35.5
|
1.0
|
NE2
|
D:HIS288
|
3.9
|
40.9
|
1.0
|
NZ
|
D:LYS167
|
4.0
|
42.2
|
1.0
|
HZ2
|
D:LYS167
|
4.1
|
42.6
|
1.0
|
O6
|
D:CAP500
|
4.1
|
35.9
|
1.0
|
CA
|
D:ASP194
|
4.1
|
34.3
|
1.0
|
CB
|
D:ASP194
|
4.2
|
36.0
|
1.0
|
CG
|
D:GLU195
|
4.2
|
41.1
|
1.0
|
NZ
|
D:KCX192
|
4.3
|
37.0
|
1.0
|
HG12
|
D:ILE165
|
4.3
|
42.0
|
1.0
|
HZ1
|
D:LYS167
|
4.3
|
42.7
|
1.0
|
HD3
|
D:PRO196
|
4.3
|
41.3
|
1.0
|
C4
|
D:CAP500
|
4.4
|
40.5
|
1.0
|
C1
|
D:CAP500
|
4.4
|
38.8
|
1.0
|
CG2
|
D:ILE165
|
4.4
|
40.9
|
1.0
|
C
|
D:ASP194
|
4.4
|
36.5
|
1.0
|
CB
|
D:GLU195
|
4.4
|
34.0
|
1.0
|
H4
|
D:CAP500
|
4.5
|
41.1
|
1.0
|
H52
|
D:CAP500
|
4.5
|
38.2
|
1.0
|
HE1
|
D:HIS288
|
4.5
|
40.8
|
1.0
|
CE1
|
D:HIS288
|
4.6
|
40.4
|
1.0
|
CA
|
D:GLU195
|
4.6
|
33.1
|
1.0
|
HG22
|
D:ILE165
|
4.7
|
42.3
|
1.0
|
O1
|
D:CAP500
|
4.7
|
41.4
|
1.0
|
H12
|
D:CAP500
|
4.8
|
37.9
|
1.0
|
HG3
|
D:LYS169
|
4.8
|
48.3
|
1.0
|
HG3
|
D:GLU195
|
4.8
|
41.1
|
1.0
|
HB3
|
D:ASP194
|
4.8
|
34.6
|
1.0
|
HG23
|
D:ILE165
|
4.8
|
39.5
|
1.0
|
CD2
|
D:HIS288
|
4.8
|
41.2
|
1.0
|
C5
|
D:CAP500
|
4.9
|
38.7
|
1.0
|
HD13
|
D:ILE165
|
4.9
|
46.8
|
1.0
|
HB2
|
D:ASP194
|
4.9
|
35.2
|
1.0
|
HG2
|
D:GLU195
|
4.9
|
40.2
|
1.0
|
H11
|
D:CAP500
|
5.0
|
38.9
|
1.0
|
H51
|
D:CAP500
|
5.0
|
38.4
|
1.0
|
CG
|
C:ASN112
|
5.0
|
50.8
|
1.0
|
|
Magnesium binding site 5 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 5 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg501
b:33.9
occ:1.00
|
HO3
|
E:CAP500
|
1.5
|
38.2
|
1.0
|
OD1
|
E:ASP194
|
1.9
|
37.8
|
1.0
|
OE1
|
E:GLU195
|
1.9
|
30.4
|
1.0
|
OQ2
|
E:KCX192
|
2.0
|
33.8
|
1.0
|
O7
|
E:CAP500
|
2.2
|
34.2
|
1.0
|
O2
|
E:CAP500
|
2.3
|
45.2
|
1.0
|
O3
|
E:CAP500
|
2.3
|
38.0
|
1.0
|
H
|
E:GLU195
|
2.7
|
33.9
|
1.0
|
HO2
|
E:CAP500
|
2.7
|
45.4
|
1.0
|
C2
|
E:CAP500
|
2.9
|
38.0
|
1.0
|
C
|
E:CAP500
|
2.9
|
33.4
|
1.0
|
HD21
|
F:ASN112
|
3.0
|
38.3
|
1.0
|
CX
|
E:KCX192
|
3.0
|
34.7
|
1.0
|
CD
|
E:GLU195
|
3.0
|
43.0
|
1.0
|
C3
|
E:CAP500
|
3.1
|
36.1
|
1.0
|
CG
|
E:ASP194
|
3.1
|
36.4
|
1.0
|
HZ3
|
E:LYS167
|
3.2
|
30.8
|
1.0
|
HE2
|
E:HIS288
|
3.3
|
38.4
|
1.0
|
HG21
|
E:ILE165
|
3.3
|
30.9
|
1.0
|
OQ1
|
E:KCX192
|
3.3
|
35.6
|
1.0
|
HA
|
E:ASP194
|
3.4
|
34.8
|
1.0
|
HZ2
|
E:LYS169
|
3.4
|
38.7
|
1.0
|
H3
|
E:CAP500
|
3.5
|
34.0
|
1.0
|
OE2
|
E:GLU195
|
3.6
|
41.5
|
1.0
|
HZ3
|
E:LYS169
|
3.6
|
38.3
|
1.0
|
N
|
E:GLU195
|
3.7
|
34.1
|
1.0
|
ND2
|
F:ASN112
|
3.7
|
38.0
|
1.0
|
HZ1
|
E:LYS169
|
3.7
|
36.9
|
1.0
|
HD22
|
F:ASN112
|
3.7
|
39.6
|
1.0
|
NZ
|
E:LYS169
|
3.8
|
38.1
|
1.0
|
OD2
|
E:ASP194
|
3.8
|
40.0
|
1.0
|
HB3
|
E:GLU195
|
3.9
|
33.8
|
1.0
|
NE2
|
E:HIS288
|
4.0
|
38.1
|
1.0
|
NZ
|
E:LYS167
|
4.0
|
31.7
|
1.0
|
HZ2
|
E:LYS167
|
4.1
|
31.4
|
1.0
|
CA
|
E:ASP194
|
4.1
|
33.2
|
1.0
|
O6
|
E:CAP500
|
4.1
|
36.2
|
1.0
|
CB
|
E:ASP194
|
4.2
|
33.8
|
1.0
|
CG
|
E:GLU195
|
4.2
|
35.3
|
1.0
|
NZ
|
E:KCX192
|
4.3
|
34.3
|
1.0
|
HG12
|
E:ILE165
|
4.3
|
33.5
|
1.0
|
HD3
|
E:PRO196
|
4.3
|
38.6
|
1.0
|
C1
|
E:CAP500
|
4.3
|
37.8
|
1.0
|
HZ1
|
E:LYS167
|
4.3
|
33.0
|
1.0
|
CG2
|
E:ILE165
|
4.4
|
31.7
|
1.0
|
C
|
E:ASP194
|
4.4
|
35.1
|
1.0
|
CB
|
E:GLU195
|
4.4
|
34.5
|
1.0
|
C4
|
E:CAP500
|
4.4
|
39.7
|
1.0
|
HE1
|
E:HIS288
|
4.4
|
38.0
|
1.0
|
CE1
|
E:HIS288
|
4.5
|
37.6
|
1.0
|
H4
|
E:CAP500
|
4.6
|
40.0
|
1.0
|
CA
|
E:GLU195
|
4.6
|
34.5
|
1.0
|
H52
|
E:CAP500
|
4.7
|
41.8
|
1.0
|
H12
|
E:CAP500
|
4.7
|
37.5
|
1.0
|
HG22
|
E:ILE165
|
4.7
|
31.7
|
1.0
|
O1
|
E:CAP500
|
4.7
|
35.9
|
1.0
|
HG3
|
E:LYS169
|
4.8
|
39.1
|
1.0
|
HG3
|
E:GLU195
|
4.8
|
33.7
|
1.0
|
HG23
|
E:ILE165
|
4.8
|
32.5
|
1.0
|
HB3
|
E:ASP194
|
4.8
|
34.5
|
1.0
|
O
|
F:HOH679
|
4.9
|
35.2
|
1.0
|
CD2
|
E:HIS288
|
4.9
|
37.7
|
1.0
|
HD13
|
E:ILE165
|
4.9
|
39.9
|
1.0
|
HB2
|
E:ASP194
|
4.9
|
34.4
|
1.0
|
HG2
|
E:GLU195
|
4.9
|
36.3
|
1.0
|
CG
|
F:ASN112
|
4.9
|
45.2
|
1.0
|
H11
|
E:CAP500
|
5.0
|
36.6
|
1.0
|
C5
|
E:CAP500
|
5.0
|
40.4
|
1.0
|
|
Magnesium binding site 6 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 6 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg501
b:39.2
occ:1.00
|
HO3
|
F:CAP500
|
1.5
|
45.1
|
1.0
|
OD1
|
F:ASP194
|
1.9
|
35.2
|
1.0
|
OE1
|
F:GLU195
|
2.0
|
32.7
|
1.0
|
OQ1
|
F:KCX192
|
2.0
|
36.4
|
1.0
|
O7
|
F:CAP500
|
2.2
|
36.4
|
1.0
|
O2
|
F:CAP500
|
2.2
|
40.4
|
1.0
|
O3
|
F:CAP500
|
2.3
|
44.9
|
1.0
|
HO2
|
F:CAP500
|
2.7
|
40.0
|
1.0
|
H
|
F:GLU195
|
2.7
|
37.7
|
1.0
|
C2
|
F:CAP500
|
2.8
|
41.8
|
1.0
|
C
|
F:CAP500
|
2.9
|
41.7
|
1.0
|
HD21
|
E:ASN112
|
3.0
|
42.2
|
1.0
|
CD
|
F:GLU195
|
3.1
|
48.3
|
1.0
|
CX
|
F:KCX192
|
3.1
|
37.7
|
1.0
|
C3
|
F:CAP500
|
3.1
|
40.2
|
1.0
|
CG
|
F:ASP194
|
3.1
|
40.4
|
1.0
|
HZ3
|
F:LYS167
|
3.1
|
39.6
|
1.0
|
HG21
|
F:ILE165
|
3.3
|
35.0
|
1.0
|
HE2
|
F:HIS288
|
3.3
|
34.6
|
1.0
|
OQ2
|
F:KCX192
|
3.4
|
38.6
|
1.0
|
HZ2
|
F:LYS169
|
3.4
|
39.1
|
1.0
|
HA
|
F:ASP194
|
3.4
|
35.8
|
1.0
|
H3
|
F:CAP500
|
3.5
|
39.1
|
1.0
|
HZ3
|
F:LYS169
|
3.5
|
40.4
|
1.0
|
OE2
|
F:GLU195
|
3.6
|
40.1
|
1.0
|
HZ1
|
F:LYS169
|
3.7
|
41.9
|
1.0
|
N
|
F:GLU195
|
3.7
|
37.8
|
1.0
|
NZ
|
F:LYS169
|
3.7
|
40.3
|
1.0
|
ND2
|
E:ASN112
|
3.7
|
42.8
|
1.0
|
HD22
|
E:ASN112
|
3.8
|
43.6
|
1.0
|
OD2
|
F:ASP194
|
3.8
|
42.1
|
1.0
|
HB3
|
F:GLU195
|
3.9
|
39.2
|
1.0
|
NZ
|
F:LYS167
|
4.0
|
40.5
|
1.0
|
NE2
|
F:HIS288
|
4.0
|
35.6
|
1.0
|
HZ2
|
F:LYS167
|
4.0
|
41.6
|
1.0
|
O6
|
F:CAP500
|
4.1
|
46.3
|
1.0
|
CA
|
F:ASP194
|
4.1
|
33.8
|
1.0
|
CB
|
F:ASP194
|
4.2
|
33.6
|
1.0
|
HG12
|
F:ILE165
|
4.3
|
35.4
|
1.0
|
CG
|
F:GLU195
|
4.3
|
40.6
|
1.0
|
HZ1
|
F:LYS167
|
4.3
|
41.2
|
1.0
|
C1
|
F:CAP500
|
4.3
|
41.9
|
1.0
|
NZ
|
F:KCX192
|
4.3
|
36.2
|
1.0
|
HD3
|
F:PRO196
|
4.3
|
38.2
|
1.0
|
CG2
|
F:ILE165
|
4.4
|
36.3
|
1.0
|
C4
|
F:CAP500
|
4.4
|
42.0
|
1.0
|
C
|
F:ASP194
|
4.4
|
40.0
|
1.0
|
HE1
|
F:HIS288
|
4.4
|
37.4
|
1.0
|
CB
|
F:GLU195
|
4.5
|
37.9
|
1.0
|
H4
|
F:CAP500
|
4.5
|
41.8
|
1.0
|
CE1
|
F:HIS288
|
4.6
|
35.5
|
1.0
|
O1
|
F:CAP500
|
4.7
|
39.7
|
1.0
|
H11
|
F:CAP500
|
4.7
|
41.9
|
1.0
|
H52
|
F:CAP500
|
4.7
|
43.3
|
1.0
|
HG22
|
F:ILE165
|
4.7
|
36.9
|
1.0
|
CA
|
F:GLU195
|
4.7
|
36.9
|
1.0
|
HG3
|
F:LYS169
|
4.8
|
44.5
|
1.0
|
HG23
|
F:ILE165
|
4.8
|
37.2
|
1.0
|
HB3
|
F:ASP194
|
4.8
|
34.2
|
1.0
|
HG3
|
F:GLU195
|
4.8
|
40.6
|
1.0
|
HD13
|
F:ILE165
|
4.9
|
36.7
|
1.0
|
H12
|
F:CAP500
|
4.9
|
41.7
|
1.0
|
CD2
|
F:HIS288
|
4.9
|
35.9
|
1.0
|
HB2
|
F:ASP194
|
4.9
|
32.3
|
1.0
|
CG
|
E:ASN112
|
4.9
|
47.7
|
1.0
|
C5
|
F:CAP500
|
5.0
|
42.8
|
1.0
|
HG2
|
F:GLU195
|
5.0
|
40.8
|
1.0
|
O
|
F:HOH642
|
5.0
|
37.6
|
1.0
|
H51
|
F:CAP500
|
5.0
|
42.0
|
1.0
|
|
Magnesium binding site 7 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 7 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg501
b:40.6
occ:1.00
|
HO3
|
G:CAP500
|
1.5
|
36.0
|
1.0
|
OD1
|
G:ASP194
|
1.9
|
39.1
|
1.0
|
OQ2
|
G:KCX192
|
2.0
|
38.5
|
1.0
|
OE1
|
G:GLU195
|
2.0
|
35.5
|
1.0
|
O6
|
G:CAP500
|
2.2
|
32.3
|
1.0
|
O2
|
G:CAP500
|
2.2
|
42.0
|
1.0
|
O3
|
G:CAP500
|
2.3
|
35.4
|
1.0
|
H
|
G:GLU195
|
2.7
|
36.4
|
1.0
|
HO2
|
G:CAP500
|
2.7
|
41.6
|
1.0
|
C2
|
G:CAP500
|
2.9
|
36.2
|
1.0
|
C
|
G:CAP500
|
2.9
|
35.7
|
1.0
|
CX
|
G:KCX192
|
3.0
|
37.3
|
1.0
|
HD21
|
H:ASN112
|
3.1
|
35.3
|
1.0
|
CD
|
G:GLU195
|
3.1
|
39.8
|
1.0
|
CG
|
G:ASP194
|
3.1
|
40.1
|
1.0
|
C3
|
G:CAP500
|
3.1
|
32.1
|
1.0
|
HZ3
|
G:LYS167
|
3.2
|
39.1
|
1.0
|
HG21
|
G:ILE165
|
3.3
|
34.8
|
1.0
|
OQ1
|
G:KCX192
|
3.3
|
38.3
|
1.0
|
HE2
|
G:HIS288
|
3.3
|
37.8
|
1.0
|
HA
|
G:ASP194
|
3.4
|
37.8
|
1.0
|
HZ2
|
G:LYS169
|
3.4
|
38.6
|
1.0
|
H3
|
G:CAP500
|
3.5
|
31.5
|
1.0
|
HZ3
|
G:LYS169
|
3.6
|
40.3
|
1.0
|
OE2
|
G:GLU195
|
3.6
|
38.6
|
1.0
|
N
|
G:GLU195
|
3.7
|
36.1
|
1.0
|
HZ1
|
G:LYS169
|
3.7
|
40.7
|
1.0
|
OD2
|
G:ASP194
|
3.8
|
43.1
|
1.0
|
NZ
|
G:LYS169
|
3.8
|
39.6
|
1.0
|
ND2
|
H:ASN112
|
3.8
|
35.7
|
1.0
|
HD22
|
H:ASN112
|
3.8
|
36.2
|
1.0
|
HB3
|
G:GLU195
|
3.9
|
39.0
|
1.0
|
NE2
|
G:HIS288
|
4.0
|
37.3
|
1.0
|
NZ
|
G:LYS167
|
4.0
|
40.1
|
1.0
|
HZ2
|
G:LYS167
|
4.0
|
41.2
|
1.0
|
CA
|
G:ASP194
|
4.1
|
35.0
|
1.0
|
O7
|
G:CAP500
|
4.2
|
39.2
|
1.0
|
CB
|
G:ASP194
|
4.2
|
36.1
|
1.0
|
NZ
|
G:KCX192
|
4.2
|
33.9
|
1.0
|
HG12
|
G:ILE165
|
4.2
|
37.6
|
1.0
|
CG
|
G:GLU195
|
4.2
|
36.6
|
1.0
|
HD3
|
G:PRO196
|
4.3
|
35.5
|
1.0
|
C1
|
G:CAP500
|
4.3
|
36.5
|
1.0
|
CG2
|
G:ILE165
|
4.3
|
36.3
|
1.0
|
HZ1
|
G:LYS167
|
4.3
|
40.0
|
1.0
|
C
|
G:ASP194
|
4.4
|
38.2
|
1.0
|
CB
|
G:GLU195
|
4.4
|
37.2
|
1.0
|
C4
|
G:CAP500
|
4.4
|
34.1
|
1.0
|
HE1
|
G:HIS288
|
4.4
|
36.4
|
1.0
|
CE1
|
G:HIS288
|
4.5
|
36.1
|
1.0
|
H4
|
G:CAP500
|
4.6
|
32.8
|
1.0
|
CA
|
G:GLU195
|
4.6
|
36.1
|
1.0
|
HG22
|
G:ILE165
|
4.7
|
36.7
|
1.0
|
H12
|
G:CAP500
|
4.7
|
35.4
|
1.0
|
H52
|
G:CAP500
|
4.7
|
33.3
|
1.0
|
O1
|
G:CAP500
|
4.7
|
37.6
|
1.0
|
HG23
|
G:ILE165
|
4.8
|
37.3
|
1.0
|
HG3
|
G:LYS169
|
4.8
|
46.0
|
1.0
|
HB3
|
G:ASP194
|
4.8
|
37.2
|
1.0
|
HG3
|
G:GLU195
|
4.8
|
33.5
|
1.0
|
HD13
|
G:ILE165
|
4.9
|
36.3
|
1.0
|
CD2
|
G:HIS288
|
4.9
|
37.4
|
1.0
|
HB2
|
G:ASP194
|
4.9
|
37.1
|
1.0
|
HG2
|
G:GLU195
|
4.9
|
38.5
|
1.0
|
H11
|
G:CAP500
|
5.0
|
36.4
|
1.0
|
C5
|
G:CAP500
|
5.0
|
34.1
|
1.0
|
|
Magnesium binding site 8 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 8 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg501
b:30.6
occ:1.00
|
HO3
|
H:CAP500
|
1.5
|
33.9
|
1.0
|
OD1
|
H:ASP194
|
1.9
|
34.8
|
1.0
|
OE1
|
H:GLU195
|
2.0
|
32.9
|
1.0
|
O6
|
H:CAP500
|
2.1
|
34.8
|
1.0
|
OQ1
|
H:KCX192
|
2.1
|
29.7
|
1.0
|
O2
|
H:CAP500
|
2.2
|
34.1
|
1.0
|
O3
|
H:CAP500
|
2.3
|
32.7
|
1.0
|
HO2
|
H:CAP500
|
2.7
|
35.6
|
1.0
|
C
|
H:CAP500
|
2.8
|
33.0
|
1.0
|
C2
|
H:CAP500
|
2.8
|
34.3
|
1.0
|
H
|
H:GLU195
|
2.8
|
35.0
|
1.0
|
HD21
|
G:ASN112
|
3.0
|
34.5
|
1.0
|
HZ3
|
H:LYS167
|
3.1
|
38.9
|
1.0
|
C3
|
H:CAP500
|
3.1
|
30.0
|
1.0
|
CG
|
H:ASP194
|
3.1
|
36.2
|
1.0
|
CD
|
H:GLU195
|
3.1
|
44.5
|
1.0
|
CX
|
H:KCX192
|
3.1
|
31.8
|
1.0
|
HG21
|
H:ILE165
|
3.3
|
36.5
|
1.0
|
HZ2
|
H:LYS169
|
3.3
|
40.1
|
1.0
|
OQ2
|
H:KCX192
|
3.4
|
33.3
|
1.0
|
HA
|
H:ASP194
|
3.4
|
29.4
|
1.0
|
HZ3
|
H:LYS169
|
3.5
|
39.8
|
1.0
|
H3
|
H:CAP500
|
3.5
|
27.9
|
1.0
|
OE2
|
H:GLU195
|
3.6
|
47.6
|
1.0
|
HZ1
|
H:LYS169
|
3.6
|
40.2
|
1.0
|
NZ
|
H:LYS169
|
3.7
|
40.1
|
1.0
|
OD2
|
H:ASP194
|
3.7
|
41.6
|
1.0
|
HD22
|
G:ASN112
|
3.7
|
34.7
|
1.0
|
ND2
|
G:ASN112
|
3.7
|
34.0
|
1.0
|
N
|
H:GLU195
|
3.8
|
34.3
|
1.0
|
NZ
|
H:LYS167
|
3.9
|
38.2
|
1.0
|
HZ2
|
H:LYS167
|
3.9
|
38.2
|
1.0
|
O7
|
H:CAP500
|
4.0
|
29.8
|
1.0
|
HB3
|
H:GLU195
|
4.0
|
38.1
|
1.0
|
NE2
|
H:HIS288
|
4.1
|
34.0
|
1.0
|
CA
|
H:ASP194
|
4.2
|
29.9
|
1.0
|
HZ1
|
H:LYS167
|
4.2
|
37.5
|
1.0
|
CB
|
H:ASP194
|
4.2
|
32.7
|
1.0
|
C1
|
H:CAP500
|
4.2
|
36.4
|
1.0
|
HG12
|
H:ILE165
|
4.3
|
29.9
|
1.0
|
CG
|
H:GLU195
|
4.3
|
42.6
|
1.0
|
HD3
|
H:PRO196
|
4.4
|
38.4
|
1.0
|
CG2
|
H:ILE165
|
4.4
|
34.0
|
1.0
|
NZ
|
H:KCX192
|
4.4
|
33.6
|
1.0
|
C4
|
H:CAP500
|
4.4
|
35.3
|
1.0
|
C
|
H:ASP194
|
4.5
|
34.6
|
1.0
|
HE1
|
H:HIS288
|
4.5
|
31.6
|
1.0
|
H4
|
H:CAP500
|
4.5
|
35.0
|
1.0
|
CB
|
H:GLU195
|
4.5
|
37.8
|
1.0
|
O1
|
H:CAP500
|
4.6
|
34.9
|
1.0
|
H12
|
H:CAP500
|
4.6
|
33.1
|
1.0
|
CE1
|
H:HIS288
|
4.6
|
33.4
|
1.0
|
HG22
|
H:ILE165
|
4.7
|
33.6
|
1.0
|
H52
|
H:CAP500
|
4.7
|
35.6
|
1.0
|
HG3
|
H:LYS169
|
4.8
|
38.1
|
1.0
|
CA
|
H:GLU195
|
4.8
|
36.2
|
1.0
|
HB3
|
H:ASP194
|
4.8
|
31.1
|
1.0
|
HG23
|
H:ILE165
|
4.8
|
33.8
|
1.0
|
HD13
|
H:ILE165
|
4.8
|
30.2
|
1.0
|
O
|
G:HOH665
|
4.8
|
31.8
|
1.0
|
H11
|
H:CAP500
|
4.9
|
36.5
|
1.0
|
O
|
G:HOH674
|
4.9
|
41.9
|
1.0
|
HG3
|
H:GLU195
|
4.9
|
43.0
|
1.0
|
HB2
|
H:ASP194
|
4.9
|
34.3
|
1.0
|
HE2
|
H:LYS167
|
5.0
|
35.4
|
1.0
|
CG
|
G:ASN112
|
5.0
|
38.2
|
1.0
|
C5
|
H:CAP500
|
5.0
|
33.3
|
1.0
|
|
Magnesium binding site 9 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 9 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 9 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Mg501
b:38.0
occ:1.00
|
HO3
|
I:CAP500
|
1.5
|
39.8
|
1.0
|
OQ1
|
I:KCX192
|
1.9
|
32.9
|
1.0
|
OD1
|
I:ASP194
|
1.9
|
39.3
|
1.0
|
OE1
|
I:GLU195
|
2.0
|
32.6
|
1.0
|
O2
|
I:CAP500
|
2.2
|
38.6
|
1.0
|
O3
|
I:CAP500
|
2.3
|
40.8
|
1.0
|
O6
|
I:CAP500
|
2.3
|
39.0
|
1.0
|
HO2
|
I:CAP500
|
2.6
|
37.9
|
1.0
|
H
|
I:GLU195
|
2.7
|
30.5
|
1.0
|
C2
|
I:CAP500
|
2.8
|
40.1
|
1.0
|
C
|
I:CAP500
|
2.9
|
40.2
|
1.0
|
CX
|
I:KCX192
|
2.9
|
32.4
|
1.0
|
C3
|
I:CAP500
|
3.1
|
38.6
|
1.0
|
HD21
|
J:ASN112
|
3.1
|
39.3
|
1.0
|
CG
|
I:ASP194
|
3.1
|
42.5
|
1.0
|
HZ3
|
I:LYS167
|
3.1
|
35.9
|
1.0
|
CD
|
I:GLU195
|
3.1
|
45.4
|
1.0
|
HG21
|
I:ILE165
|
3.2
|
36.9
|
1.0
|
OQ2
|
I:KCX192
|
3.2
|
32.7
|
1.0
|
HE2
|
I:HIS288
|
3.3
|
41.1
|
1.0
|
HA
|
I:ASP194
|
3.3
|
29.9
|
1.0
|
H3
|
I:CAP500
|
3.4
|
38.2
|
1.0
|
HZ2
|
I:LYS169
|
3.5
|
47.8
|
1.0
|
HZ3
|
I:LYS169
|
3.6
|
48.9
|
1.0
|
N
|
I:GLU195
|
3.7
|
30.9
|
1.0
|
OE2
|
I:GLU195
|
3.7
|
45.2
|
1.0
|
OD2
|
I:ASP194
|
3.8
|
49.6
|
1.0
|
HZ1
|
I:LYS169
|
3.8
|
48.6
|
1.0
|
NZ
|
I:LYS169
|
3.8
|
48.2
|
1.0
|
ND2
|
J:ASN112
|
3.9
|
38.1
|
1.0
|
HD22
|
J:ASN112
|
3.9
|
38.3
|
1.0
|
HB3
|
I:GLU195
|
3.9
|
30.9
|
1.0
|
NE2
|
I:HIS288
|
3.9
|
40.0
|
1.0
|
NZ
|
I:LYS167
|
4.0
|
37.2
|
1.0
|
HZ2
|
I:LYS167
|
4.0
|
36.5
|
1.0
|
CA
|
I:ASP194
|
4.1
|
30.7
|
1.0
|
HG12
|
I:ILE165
|
4.2
|
35.4
|
1.0
|
O7
|
I:CAP500
|
4.2
|
41.4
|
1.0
|
CB
|
I:ASP194
|
4.2
|
31.7
|
1.0
|
NZ
|
I:KCX192
|
4.2
|
34.5
|
1.0
|
C1
|
I:CAP500
|
4.3
|
39.4
|
1.0
|
CG2
|
I:ILE165
|
4.3
|
37.3
|
1.0
|
CG
|
I:GLU195
|
4.3
|
39.5
|
1.0
|
HZ1
|
I:LYS167
|
4.3
|
37.9
|
1.0
|
C4
|
I:CAP500
|
4.4
|
40.8
|
1.0
|
HD3
|
I:PRO196
|
4.4
|
39.5
|
1.0
|
C
|
I:ASP194
|
4.4
|
35.1
|
1.0
|
CB
|
I:GLU195
|
4.5
|
31.2
|
1.0
|
HE1
|
I:HIS288
|
4.5
|
40.7
|
1.0
|
CE1
|
I:HIS288
|
4.5
|
39.6
|
1.0
|
H4
|
I:CAP500
|
4.6
|
40.3
|
1.0
|
HG22
|
I:ILE165
|
4.6
|
39.2
|
1.0
|
H11
|
I:CAP500
|
4.6
|
38.3
|
1.0
|
O1
|
I:CAP500
|
4.7
|
41.4
|
1.0
|
CA
|
I:GLU195
|
4.7
|
30.2
|
1.0
|
H52
|
I:CAP500
|
4.7
|
45.3
|
1.0
|
HG23
|
I:ILE165
|
4.7
|
36.5
|
1.0
|
HD13
|
I:ILE165
|
4.8
|
35.3
|
1.0
|
HB3
|
I:ASP194
|
4.8
|
30.5
|
1.0
|
CD2
|
I:HIS288
|
4.9
|
40.1
|
1.0
|
HG3
|
I:LYS169
|
4.9
|
40.8
|
1.0
|
H12
|
I:CAP500
|
4.9
|
40.5
|
1.0
|
HG3
|
I:GLU195
|
4.9
|
41.1
|
1.0
|
HB2
|
I:ASP194
|
4.9
|
31.1
|
1.0
|
C5
|
I:CAP500
|
5.0
|
44.7
|
1.0
|
H51
|
I:CAP500
|
5.0
|
44.8
|
1.0
|
HE2
|
I:LYS167
|
5.0
|
30.2
|
1.0
|
|
Magnesium binding site 10 out
of 12 in 5hat
Go back to
Magnesium Binding Sites List in 5hat
Magnesium binding site 10 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 10 of Structure Function Studies of R. Palustris Rubisco (S59F/M331A Mutant; Cabp-Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Mg501
b:38.6
occ:1.00
|
HO3
|
J:CAP500
|
1.5
|
46.3
|
1.0
|
OD1
|
J:ASP194
|
1.9
|
40.9
|
1.0
|
OE1
|
J:GLU195
|
1.9
|
41.5
|
1.0
|
OQ2
|
J:KCX192
|
2.1
|
34.5
|
1.0
|
O7
|
J:CAP500
|
2.2
|
37.8
|
1.0
|
O2
|
J:CAP500
|
2.3
|
48.3
|
1.0
|
O3
|
J:CAP500
|
2.3
|
47.5
|
1.0
|
H
|
J:GLU195
|
2.7
|
34.9
|
1.0
|
HO2
|
J:CAP500
|
2.7
|
48.4
|
1.0
|
C2
|
J:CAP500
|
2.9
|
45.0
|
1.0
|
C
|
J:CAP500
|
2.9
|
39.2
|
1.0
|
CD
|
J:GLU195
|
3.0
|
48.2
|
1.0
|
HD21
|
I:ASN112
|
3.0
|
37.6
|
1.0
|
C3
|
J:CAP500
|
3.1
|
47.9
|
1.0
|
CX
|
J:KCX192
|
3.1
|
36.3
|
1.0
|
CG
|
J:ASP194
|
3.1
|
41.4
|
1.0
|
HZ3
|
J:LYS169
|
3.1
|
46.7
|
1.0
|
HZ3
|
J:LYS167
|
3.2
|
38.9
|
1.0
|
HE2
|
J:HIS288
|
3.3
|
44.2
|
1.0
|
HG21
|
J:ILE165
|
3.4
|
40.0
|
1.0
|
OQ1
|
J:KCX192
|
3.4
|
36.9
|
1.0
|
HA
|
J:ASP194
|
3.4
|
34.7
|
1.0
|
H3
|
J:CAP500
|
3.5
|
48.0
|
1.0
|
OE2
|
J:GLU195
|
3.5
|
37.5
|
1.0
|
HZ1
|
J:LYS169
|
3.6
|
48.0
|
1.0
|
N
|
J:GLU195
|
3.7
|
34.5
|
1.0
|
ND2
|
I:ASN112
|
3.8
|
38.8
|
1.0
|
NZ
|
J:LYS169
|
3.8
|
47.5
|
1.0
|
HD22
|
I:ASN112
|
3.8
|
39.5
|
1.0
|
OD2
|
J:ASP194
|
3.8
|
38.0
|
1.0
|
HB3
|
J:GLU195
|
3.9
|
37.9
|
1.0
|
NE2
|
J:HIS288
|
4.0
|
43.5
|
1.0
|
NZ
|
J:LYS167
|
4.0
|
40.8
|
1.0
|
HZ2
|
J:LYS167
|
4.0
|
40.5
|
1.0
|
HZ2
|
J:LYS169
|
4.0
|
46.5
|
1.0
|
O6
|
J:CAP500
|
4.1
|
38.9
|
1.0
|
CA
|
J:ASP194
|
4.1
|
34.5
|
1.0
|
CB
|
J:ASP194
|
4.2
|
36.1
|
1.0
|
CG
|
J:GLU195
|
4.2
|
43.5
|
1.0
|
HZ1
|
J:LYS167
|
4.3
|
40.9
|
1.0
|
HG12
|
J:ILE165
|
4.3
|
41.3
|
1.0
|
HD3
|
J:PRO196
|
4.3
|
43.2
|
1.0
|
NZ
|
J:KCX192
|
4.3
|
36.8
|
1.0
|
C1
|
J:CAP500
|
4.3
|
41.4
|
1.0
|
C4
|
J:CAP500
|
4.4
|
50.2
|
1.0
|
C
|
J:ASP194
|
4.4
|
40.5
|
1.0
|
CG2
|
J:ILE165
|
4.4
|
39.7
|
1.0
|
HE1
|
J:HIS288
|
4.4
|
41.5
|
1.0
|
CB
|
J:GLU195
|
4.4
|
36.2
|
1.0
|
H4
|
J:CAP500
|
4.5
|
51.4
|
1.0
|
CE1
|
J:HIS288
|
4.5
|
42.2
|
1.0
|
CA
|
J:GLU195
|
4.7
|
34.5
|
1.0
|
H52
|
J:CAP500
|
4.7
|
44.8
|
1.0
|
H12
|
J:CAP500
|
4.7
|
40.7
|
1.0
|
O1
|
J:CAP500
|
4.7
|
41.6
|
1.0
|
HG22
|
J:ILE165
|
4.7
|
38.8
|
1.0
|
HG3
|
J:GLU195
|
4.8
|
42.1
|
1.0
|
HB3
|
J:ASP194
|
4.8
|
35.1
|
1.0
|
HG23
|
J:ILE165
|
4.9
|
39.0
|
1.0
|
HD13
|
J:ILE165
|
4.9
|
47.4
|
1.0
|
O
|
I:HOH663
|
4.9
|
39.3
|
1.0
|
CD2
|
J:HIS288
|
4.9
|
43.2
|
1.0
|
HG3
|
J:LYS169
|
4.9
|
38.3
|
1.0
|
HG2
|
J:GLU195
|
4.9
|
44.0
|
1.0
|
H11
|
J:CAP500
|
4.9
|
40.4
|
1.0
|
HB2
|
J:ASP194
|
4.9
|
36.4
|
1.0
|
C5
|
J:CAP500
|
5.0
|
46.0
|
1.0
|
CG
|
I:ASN112
|
5.0
|
43.6
|
1.0
|
|
Reference:
M.A.Arbing,
S.Satagopan,
V.A.Varaljay,
J.G.Leong,
F.R.Tabita.
Structure Function Studies of R. Palustris Rubisco. To Be Published.
Page generated: Sun Sep 29 15:45:55 2024
|