Magnesium in PDB 5han: Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)
Enzymatic activity of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound)
All present enzymatic activity of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound):
4.1.1.39;
Protein crystallography data
The structure of Structure Function Studies of R. Palustris Rubisco (S59F Mutant; Cabp- Bound), PDB code: 5han
was solved by
M.A.Arbing,
J.G.Leong,
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 /
2.04
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
75.880,
110.370,
167.360,
89.87,
101.70,
105.00
|
R / Rfree (%)
|
19.7 /
23.7
|
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 Mutant; Cabp- Bound)
(pdb code 5han). 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 Mutant; Cabp- Bound), PDB code: 5han:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Magnesium binding site 1 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 1 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg501
b:30.6
occ:1.00
|
HO3
|
A:CAP500
|
1.4
|
35.1
|
1.0
|
OE1
|
A:GLU195
|
1.9
|
27.6
|
1.0
|
OQ2
|
A:KCX192
|
2.1
|
24.2
|
1.0
|
OD1
|
A:ASP194
|
2.1
|
41.3
|
1.0
|
O6
|
A:CAP500
|
2.1
|
32.2
|
1.0
|
O3
|
A:CAP500
|
2.2
|
34.8
|
1.0
|
O2
|
A:CAP500
|
2.2
|
42.2
|
1.0
|
HO2
|
A:CAP500
|
2.8
|
41.1
|
1.0
|
C
|
A:CAP500
|
2.8
|
35.5
|
1.0
|
C2
|
A:CAP500
|
2.8
|
38.8
|
1.0
|
H
|
A:GLU195
|
2.8
|
31.9
|
1.0
|
HD21
|
B:ASN112
|
2.8
|
37.7
|
1.0
|
HZ3
|
A:LYS169
|
3.0
|
61.6
|
1.0
|
C3
|
A:CAP500
|
3.0
|
40.5
|
1.0
|
CD
|
A:GLU195
|
3.0
|
36.8
|
1.0
|
HZ1
|
A:LYS169
|
3.1
|
61.4
|
1.0
|
CX
|
A:KCX192
|
3.2
|
27.3
|
1.0
|
HZ2
|
A:LYS167
|
3.2
|
38.0
|
1.0
|
CG
|
A:ASP194
|
3.3
|
42.2
|
1.0
|
HZ2
|
A:LYS169
|
3.3
|
61.1
|
1.0
|
HE2
|
A:HIS288
|
3.3
|
30.3
|
1.0
|
NZ
|
A:LYS169
|
3.3
|
61.3
|
1.0
|
H3
|
A:CAP500
|
3.4
|
41.5
|
1.0
|
OQ1
|
A:KCX192
|
3.5
|
28.2
|
1.0
|
HG21
|
A:ILE165
|
3.5
|
33.8
|
1.0
|
HA
|
A:ASP194
|
3.5
|
31.5
|
1.0
|
ND2
|
B:ASN112
|
3.6
|
37.8
|
1.0
|
OE2
|
A:GLU195
|
3.6
|
33.7
|
1.0
|
HD22
|
B:ASN112
|
3.6
|
37.9
|
1.0
|
N
|
A:GLU195
|
3.8
|
32.6
|
1.0
|
HB3
|
A:GLU195
|
3.9
|
34.6
|
1.0
|
NE2
|
A:HIS288
|
3.9
|
29.1
|
1.0
|
OD2
|
A:ASP194
|
4.0
|
47.3
|
1.0
|
O7
|
A:CAP500
|
4.0
|
35.7
|
1.0
|
NZ
|
A:LYS167
|
4.0
|
39.0
|
1.0
|
HE1
|
A:HIS288
|
4.1
|
30.2
|
1.0
|
HZ1
|
A:LYS167
|
4.1
|
38.9
|
1.0
|
CG
|
A:GLU195
|
4.2
|
35.0
|
1.0
|
HZ3
|
A:LYS167
|
4.2
|
40.4
|
1.0
|
CA
|
A:ASP194
|
4.2
|
30.5
|
1.0
|
C1
|
A:CAP500
|
4.3
|
33.6
|
1.0
|
C4
|
A:CAP500
|
4.3
|
42.4
|
1.0
|
CB
|
A:ASP194
|
4.3
|
28.9
|
1.0
|
CE1
|
A:HIS288
|
4.3
|
28.6
|
1.0
|
NZ
|
A:KCX192
|
4.4
|
26.6
|
1.0
|
CB
|
A:GLU195
|
4.4
|
34.3
|
1.0
|
H4
|
A:CAP500
|
4.5
|
42.4
|
1.0
|
C
|
A:ASP194
|
4.5
|
34.9
|
1.0
|
HG12
|
A:ILE165
|
4.5
|
33.6
|
1.0
|
HD3
|
A:PRO196
|
4.5
|
31.9
|
1.0
|
CG2
|
A:ILE165
|
4.6
|
33.3
|
1.0
|
H52
|
A:CAP500
|
4.6
|
40.2
|
1.0
|
H12
|
A:CAP500
|
4.6
|
33.3
|
1.0
|
O1
|
A:CAP500
|
4.7
|
32.6
|
1.0
|
CA
|
A:GLU195
|
4.7
|
32.8
|
1.0
|
HG3
|
A:GLU195
|
4.7
|
33.0
|
1.0
|
CG
|
B:ASN112
|
4.7
|
44.1
|
1.0
|
CE
|
A:LYS169
|
4.8
|
57.9
|
1.0
|
HD13
|
A:ILE165
|
4.8
|
29.0
|
1.0
|
C5
|
A:CAP500
|
4.8
|
41.3
|
1.0
|
H51
|
A:CAP500
|
4.8
|
42.0
|
1.0
|
HG3
|
A:LYS169
|
4.8
|
45.6
|
1.0
|
H11
|
A:CAP500
|
4.9
|
34.5
|
1.0
|
HG22
|
A:ILE165
|
4.9
|
33.6
|
1.0
|
CD2
|
A:HIS288
|
4.9
|
29.7
|
1.0
|
HG2
|
A:GLU195
|
4.9
|
35.0
|
1.0
|
HB3
|
A:ASP194
|
5.0
|
29.0
|
1.0
|
O
|
B:HOH683
|
5.0
|
38.5
|
1.0
|
|
Magnesium binding site 2 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 2 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg501
b:36.6
occ:1.00
|
HO3
|
B:CAP500
|
1.6
|
31.1
|
1.0
|
OD1
|
B:ASP194
|
1.9
|
29.4
|
1.0
|
OQ2
|
B:KCX192
|
1.9
|
31.6
|
1.0
|
OE1
|
B:GLU195
|
1.9
|
34.3
|
1.0
|
O6
|
B:CAP500
|
2.2
|
34.4
|
1.0
|
O2
|
B:CAP500
|
2.2
|
46.8
|
1.0
|
O3
|
B:CAP500
|
2.4
|
30.7
|
1.0
|
HO2
|
B:CAP500
|
2.7
|
48.0
|
1.0
|
H
|
B:GLU195
|
2.7
|
34.7
|
1.0
|
C2
|
B:CAP500
|
2.8
|
36.4
|
1.0
|
C
|
B:CAP500
|
2.9
|
33.1
|
1.0
|
CX
|
B:KCX192
|
3.0
|
31.9
|
1.0
|
CD
|
B:GLU195
|
3.1
|
52.1
|
1.0
|
HZ2
|
B:LYS167
|
3.1
|
32.2
|
1.0
|
HD21
|
A:ASN112
|
3.1
|
38.3
|
1.0
|
CG
|
B:ASP194
|
3.1
|
32.8
|
1.0
|
C3
|
B:CAP500
|
3.1
|
32.9
|
1.0
|
OQ1
|
B:KCX192
|
3.3
|
31.8
|
1.0
|
HZ3
|
B:LYS169
|
3.3
|
38.2
|
1.0
|
HZ2
|
B:LYS169
|
3.4
|
38.6
|
1.0
|
HA
|
B:ASP194
|
3.4
|
30.7
|
1.0
|
HG21
|
B:ILE165
|
3.4
|
24.9
|
1.0
|
H3
|
B:CAP500
|
3.5
|
34.1
|
1.0
|
OE2
|
B:GLU195
|
3.6
|
41.7
|
1.0
|
NZ
|
B:LYS169
|
3.7
|
39.4
|
1.0
|
HZ1
|
B:LYS169
|
3.7
|
40.4
|
1.0
|
N
|
B:GLU195
|
3.7
|
33.9
|
1.0
|
HD22
|
A:ASN112
|
3.7
|
38.6
|
1.0
|
ND2
|
A:ASN112
|
3.8
|
38.3
|
1.0
|
OD2
|
B:ASP194
|
3.8
|
38.0
|
1.0
|
NZ
|
B:LYS167
|
3.9
|
33.7
|
1.0
|
HB3
|
B:GLU195
|
3.9
|
34.5
|
1.0
|
HZ1
|
B:LYS167
|
4.0
|
35.7
|
1.0
|
NE2
|
B:HIS288
|
4.0
|
33.6
|
1.0
|
O7
|
B:CAP500
|
4.1
|
32.0
|
1.0
|
CA
|
B:ASP194
|
4.1
|
29.2
|
1.0
|
HZ3
|
B:LYS167
|
4.1
|
34.2
|
1.0
|
CB
|
B:ASP194
|
4.2
|
30.7
|
1.0
|
NZ
|
B:KCX192
|
4.2
|
31.2
|
1.0
|
CG
|
B:GLU195
|
4.2
|
47.6
|
1.0
|
C1
|
B:CAP500
|
4.2
|
38.0
|
1.0
|
HD3
|
B:PRO196
|
4.3
|
35.6
|
1.0
|
HE1
|
B:HIS288
|
4.3
|
32.0
|
1.0
|
C
|
B:ASP194
|
4.4
|
35.4
|
1.0
|
CB
|
B:GLU195
|
4.4
|
33.9
|
1.0
|
CG2
|
B:ILE165
|
4.4
|
27.6
|
1.0
|
C4
|
B:CAP500
|
4.5
|
31.2
|
1.0
|
CE1
|
B:HIS288
|
4.5
|
32.2
|
1.0
|
H12
|
B:CAP500
|
4.6
|
36.2
|
1.0
|
O1
|
B:CAP500
|
4.6
|
37.7
|
1.0
|
HG22
|
B:ILE165
|
4.6
|
27.4
|
1.0
|
H4
|
B:CAP500
|
4.6
|
31.1
|
1.0
|
CA
|
B:GLU195
|
4.7
|
32.5
|
1.0
|
HG3
|
B:LYS169
|
4.7
|
35.6
|
1.0
|
H52
|
B:CAP500
|
4.8
|
32.9
|
1.0
|
HG3
|
B:GLU195
|
4.8
|
48.6
|
1.0
|
HB3
|
B:ASP194
|
4.8
|
29.6
|
1.0
|
O
|
A:HOH691
|
4.8
|
39.9
|
1.0
|
HB2
|
B:ASP194
|
4.8
|
31.1
|
1.0
|
H11
|
B:CAP500
|
4.9
|
39.5
|
1.0
|
O
|
A:HOH744
|
4.9
|
40.4
|
1.0
|
HG2
|
B:GLU195
|
4.9
|
47.4
|
1.0
|
HG23
|
B:ILE165
|
5.0
|
27.6
|
1.0
|
|
Magnesium binding site 3 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 3 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg501
b:34.4
occ:1.00
|
HO3
|
C:CAP500
|
1.5
|
34.9
|
1.0
|
OD1
|
C:ASP194
|
1.9
|
29.8
|
1.0
|
OE1
|
C:GLU195
|
2.0
|
36.9
|
1.0
|
O6
|
C:CAP500
|
2.1
|
32.5
|
1.0
|
O2
|
C:CAP500
|
2.1
|
42.1
|
1.0
|
OQ2
|
C:KCX192
|
2.1
|
33.1
|
1.0
|
O3
|
C:CAP500
|
2.3
|
37.3
|
1.0
|
HO2
|
C:CAP500
|
2.7
|
42.3
|
1.0
|
C2
|
C:CAP500
|
2.7
|
38.6
|
1.0
|
C
|
C:CAP500
|
2.7
|
32.7
|
1.0
|
H
|
C:GLU195
|
2.9
|
34.2
|
1.0
|
HD21
|
D:ASN112
|
3.0
|
47.9
|
1.0
|
HZ2
|
C:LYS167
|
3.0
|
38.0
|
1.0
|
C3
|
C:CAP500
|
3.0
|
39.0
|
1.0
|
CG
|
C:ASP194
|
3.1
|
35.9
|
1.0
|
CD
|
C:GLU195
|
3.1
|
43.4
|
1.0
|
CX
|
C:KCX192
|
3.2
|
33.8
|
1.0
|
HG21
|
C:ILE165
|
3.3
|
30.6
|
1.0
|
HZ3
|
C:LYS169
|
3.4
|
54.0
|
1.0
|
OQ1
|
C:KCX192
|
3.4
|
38.3
|
1.0
|
HZ2
|
C:LYS169
|
3.4
|
54.1
|
1.0
|
H3
|
C:CAP500
|
3.4
|
39.4
|
1.0
|
HA
|
C:ASP194
|
3.5
|
32.1
|
1.0
|
OE2
|
C:GLU195
|
3.7
|
37.3
|
1.0
|
HZ1
|
C:LYS169
|
3.7
|
54.0
|
1.0
|
NZ
|
C:LYS169
|
3.7
|
53.9
|
1.0
|
HD22
|
D:ASN112
|
3.7
|
47.7
|
1.0
|
ND2
|
D:ASN112
|
3.7
|
47.7
|
1.0
|
OD2
|
C:ASP194
|
3.7
|
42.1
|
1.0
|
NZ
|
C:LYS167
|
3.8
|
40.1
|
1.0
|
N
|
C:GLU195
|
3.8
|
33.6
|
1.0
|
HZ1
|
C:LYS167
|
4.0
|
40.9
|
1.0
|
O7
|
C:CAP500
|
4.0
|
33.7
|
1.0
|
HB3
|
C:GLU195
|
4.0
|
36.1
|
1.0
|
NE2
|
C:HIS288
|
4.1
|
32.3
|
1.0
|
HZ3
|
C:LYS167
|
4.1
|
40.5
|
1.0
|
C1
|
C:CAP500
|
4.1
|
39.1
|
1.0
|
CA
|
C:ASP194
|
4.2
|
32.9
|
1.0
|
CB
|
C:ASP194
|
4.2
|
31.5
|
1.0
|
NZ
|
C:KCX192
|
4.3
|
32.0
|
1.0
|
HG12
|
C:ILE165
|
4.3
|
35.5
|
1.0
|
HE1
|
C:HIS288
|
4.3
|
32.3
|
1.0
|
CG
|
C:GLU195
|
4.3
|
41.0
|
1.0
|
C4
|
C:CAP500
|
4.4
|
39.6
|
1.0
|
CG2
|
C:ILE165
|
4.4
|
31.2
|
1.0
|
HD3
|
C:PRO196
|
4.4
|
33.2
|
1.0
|
C
|
C:ASP194
|
4.5
|
38.6
|
1.0
|
H4
|
C:CAP500
|
4.5
|
40.6
|
1.0
|
CB
|
C:GLU195
|
4.5
|
35.1
|
1.0
|
CE1
|
C:HIS288
|
4.5
|
31.7
|
1.0
|
O1
|
C:CAP500
|
4.5
|
35.9
|
1.0
|
H11
|
C:CAP500
|
4.6
|
40.0
|
1.0
|
HG22
|
C:ILE165
|
4.7
|
31.4
|
1.0
|
H52
|
C:CAP500
|
4.7
|
34.3
|
1.0
|
H12
|
C:CAP500
|
4.8
|
39.6
|
1.0
|
HG3
|
C:LYS169
|
4.8
|
32.3
|
1.0
|
CA
|
C:GLU195
|
4.8
|
33.5
|
1.0
|
HB3
|
C:ASP194
|
4.8
|
28.7
|
1.0
|
HD13
|
C:ILE165
|
4.8
|
38.9
|
1.0
|
HG23
|
C:ILE165
|
4.8
|
28.7
|
1.0
|
HG3
|
C:GLU195
|
4.9
|
40.5
|
1.0
|
HB2
|
C:ASP194
|
4.9
|
30.3
|
1.0
|
C5
|
C:CAP500
|
4.9
|
36.1
|
1.0
|
CG
|
D:ASN112
|
4.9
|
51.7
|
1.0
|
H51
|
C:CAP500
|
5.0
|
35.6
|
1.0
|
O
|
D:HOH657
|
5.0
|
50.5
|
1.0
|
HE2
|
C:LYS167
|
5.0
|
29.6
|
1.0
|
|
Magnesium binding site 4 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 4 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg501
b:35.2
occ:1.00
|
HO3
|
D:CAP500
|
1.5
|
30.4
|
1.0
|
OD1
|
D:ASP194
|
2.0
|
32.6
|
1.0
|
O2
|
D:CAP500
|
2.0
|
37.2
|
1.0
|
OQ2
|
D:KCX192
|
2.0
|
27.6
|
1.0
|
OE1
|
D:GLU195
|
2.1
|
37.6
|
1.0
|
O6
|
D:CAP500
|
2.1
|
33.4
|
1.0
|
O3
|
D:CAP500
|
2.3
|
30.3
|
1.0
|
HO2
|
D:CAP500
|
2.6
|
37.2
|
1.0
|
C2
|
D:CAP500
|
2.7
|
32.2
|
1.0
|
C
|
D:CAP500
|
2.7
|
36.3
|
1.0
|
H
|
D:GLU195
|
2.9
|
33.2
|
1.0
|
HZ2
|
D:LYS167
|
3.0
|
39.1
|
1.0
|
C3
|
D:CAP500
|
3.0
|
33.4
|
1.0
|
HD21
|
C:ASN112
|
3.0
|
34.2
|
1.0
|
CX
|
D:KCX192
|
3.1
|
32.0
|
1.0
|
CG
|
D:ASP194
|
3.1
|
33.7
|
1.0
|
HG21
|
D:ILE165
|
3.2
|
38.8
|
1.0
|
CD
|
D:GLU195
|
3.2
|
38.7
|
1.0
|
OQ1
|
D:KCX192
|
3.3
|
34.9
|
1.0
|
H3
|
D:CAP500
|
3.4
|
34.1
|
1.0
|
HZ3
|
D:LYS169
|
3.4
|
39.9
|
1.0
|
HE2
|
D:HIS288
|
3.5
|
31.8
|
1.0
|
HA
|
D:ASP194
|
3.5
|
27.6
|
1.0
|
HZ2
|
D:LYS169
|
3.5
|
39.3
|
1.0
|
OD2
|
D:ASP194
|
3.7
|
42.0
|
1.0
|
HZ1
|
D:LYS169
|
3.8
|
39.2
|
1.0
|
NZ
|
D:LYS169
|
3.8
|
39.7
|
1.0
|
OE2
|
D:GLU195
|
3.8
|
39.6
|
1.0
|
HD22
|
C:ASN112
|
3.8
|
35.2
|
1.0
|
ND2
|
C:ASN112
|
3.8
|
33.5
|
1.0
|
NZ
|
D:LYS167
|
3.8
|
41.1
|
1.0
|
N
|
D:GLU195
|
3.9
|
32.4
|
1.0
|
HZ1
|
D:LYS167
|
3.9
|
41.9
|
1.0
|
O7
|
D:CAP500
|
4.0
|
31.4
|
1.0
|
HB3
|
D:GLU195
|
4.0
|
32.5
|
1.0
|
HZ3
|
D:LYS167
|
4.0
|
42.3
|
1.0
|
NE2
|
D:HIS288
|
4.1
|
29.6
|
1.0
|
C1
|
D:CAP500
|
4.1
|
33.5
|
1.0
|
CA
|
D:ASP194
|
4.2
|
28.2
|
1.0
|
HG12
|
D:ILE165
|
4.2
|
36.5
|
1.0
|
CB
|
D:ASP194
|
4.2
|
29.6
|
1.0
|
NZ
|
D:KCX192
|
4.3
|
30.8
|
1.0
|
CG2
|
D:ILE165
|
4.3
|
38.2
|
1.0
|
C4
|
D:CAP500
|
4.3
|
33.4
|
1.0
|
HE1
|
D:HIS288
|
4.4
|
32.0
|
1.0
|
CG
|
D:GLU195
|
4.4
|
35.9
|
1.0
|
HD3
|
D:PRO196
|
4.5
|
36.7
|
1.0
|
H12
|
D:CAP500
|
4.5
|
32.0
|
1.0
|
O1
|
D:CAP500
|
4.5
|
37.6
|
1.0
|
H4
|
D:CAP500
|
4.5
|
34.7
|
1.0
|
C
|
D:ASP194
|
4.5
|
35.6
|
1.0
|
CE1
|
D:HIS288
|
4.6
|
29.9
|
1.0
|
CB
|
D:GLU195
|
4.6
|
31.7
|
1.0
|
HG22
|
D:ILE165
|
4.6
|
38.4
|
1.0
|
H52
|
D:CAP500
|
4.7
|
34.1
|
1.0
|
H11
|
D:CAP500
|
4.7
|
33.3
|
1.0
|
HD13
|
D:ILE165
|
4.7
|
34.9
|
1.0
|
HG23
|
D:ILE165
|
4.8
|
37.1
|
1.0
|
HG3
|
D:LYS169
|
4.8
|
32.3
|
1.0
|
HB3
|
D:ASP194
|
4.8
|
31.0
|
1.0
|
CA
|
D:GLU195
|
4.9
|
31.4
|
1.0
|
HE2
|
D:LYS167
|
4.9
|
43.1
|
1.0
|
HB2
|
D:ASP194
|
4.9
|
30.2
|
1.0
|
C5
|
D:CAP500
|
4.9
|
34.3
|
1.0
|
H51
|
D:CAP500
|
4.9
|
33.3
|
1.0
|
HG3
|
D:GLU195
|
5.0
|
37.5
|
1.0
|
O
|
C:HOH616
|
5.0
|
36.8
|
1.0
|
|
Magnesium binding site 5 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 5 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg501
b:25.7
occ:1.00
|
HO3
|
E:CAP500
|
1.5
|
31.2
|
1.0
|
OE1
|
E:GLU195
|
1.9
|
28.7
|
1.0
|
OD1
|
E:ASP194
|
2.0
|
33.9
|
1.0
|
OQ2
|
E:KCX192
|
2.0
|
23.6
|
1.0
|
O6
|
E:CAP500
|
2.1
|
28.7
|
1.0
|
O2
|
E:CAP500
|
2.2
|
27.7
|
1.0
|
O3
|
E:CAP500
|
2.3
|
29.8
|
1.0
|
H
|
E:GLU195
|
2.7
|
28.4
|
1.0
|
HO2
|
E:CAP500
|
2.7
|
29.2
|
1.0
|
C2
|
E:CAP500
|
2.8
|
30.7
|
1.0
|
C
|
E:CAP500
|
2.8
|
26.1
|
1.0
|
HD21
|
F:ASN112
|
2.9
|
38.3
|
1.0
|
CX
|
E:KCX192
|
3.0
|
29.0
|
1.0
|
CD
|
E:GLU195
|
3.1
|
35.4
|
1.0
|
C3
|
E:CAP500
|
3.1
|
30.4
|
1.0
|
CG
|
E:ASP194
|
3.1
|
33.5
|
1.0
|
HZ2
|
E:LYS167
|
3.2
|
30.1
|
1.0
|
OQ1
|
E:KCX192
|
3.3
|
30.7
|
1.0
|
HG21
|
E:ILE165
|
3.3
|
26.1
|
1.0
|
HA
|
E:ASP194
|
3.4
|
28.6
|
1.0
|
HZ3
|
E:LYS169
|
3.4
|
34.0
|
1.0
|
HZ2
|
E:LYS169
|
3.4
|
35.0
|
1.0
|
H3
|
E:CAP500
|
3.5
|
30.0
|
1.0
|
OE2
|
E:GLU195
|
3.6
|
42.8
|
1.0
|
ND2
|
F:ASN112
|
3.7
|
37.8
|
1.0
|
HD22
|
F:ASN112
|
3.7
|
37.9
|
1.0
|
N
|
E:GLU195
|
3.7
|
29.6
|
1.0
|
NZ
|
E:LYS169
|
3.8
|
34.6
|
1.0
|
HZ1
|
E:LYS169
|
3.8
|
34.8
|
1.0
|
OD2
|
E:ASP194
|
3.8
|
41.4
|
1.0
|
HB3
|
E:GLU195
|
3.8
|
36.3
|
1.0
|
NE2
|
E:HIS288
|
3.9
|
33.2
|
1.0
|
NZ
|
E:LYS167
|
4.0
|
30.1
|
1.0
|
O7
|
E:CAP500
|
4.1
|
25.5
|
1.0
|
HZ1
|
E:LYS167
|
4.1
|
30.1
|
1.0
|
CA
|
E:ASP194
|
4.1
|
27.8
|
1.0
|
CB
|
E:ASP194
|
4.2
|
27.6
|
1.0
|
CG
|
E:GLU195
|
4.2
|
37.0
|
1.0
|
HZ3
|
E:LYS167
|
4.2
|
30.0
|
1.0
|
NZ
|
E:KCX192
|
4.2
|
32.8
|
1.0
|
HE1
|
E:HIS288
|
4.2
|
31.7
|
1.0
|
C1
|
E:CAP500
|
4.3
|
29.7
|
1.0
|
HD3
|
E:PRO196
|
4.3
|
36.2
|
1.0
|
HG12
|
E:ILE165
|
4.3
|
21.6
|
1.0
|
CB
|
E:GLU195
|
4.4
|
35.2
|
1.0
|
C4
|
E:CAP500
|
4.4
|
30.6
|
1.0
|
CG2
|
E:ILE165
|
4.4
|
25.1
|
1.0
|
CE1
|
E:HIS288
|
4.4
|
32.1
|
1.0
|
C
|
E:ASP194
|
4.4
|
29.3
|
1.0
|
H4
|
E:CAP500
|
4.6
|
30.1
|
1.0
|
H12
|
E:CAP500
|
4.6
|
28.2
|
1.0
|
CA
|
E:GLU195
|
4.7
|
32.1
|
1.0
|
O1
|
E:CAP500
|
4.7
|
26.8
|
1.0
|
H52
|
E:CAP500
|
4.7
|
32.8
|
1.0
|
O
|
F:HOH677
|
4.7
|
32.5
|
1.0
|
HG22
|
E:ILE165
|
4.7
|
24.2
|
1.0
|
HG3
|
E:LYS169
|
4.8
|
41.0
|
1.0
|
HG3
|
E:GLU195
|
4.8
|
37.3
|
1.0
|
HB3
|
E:ASP194
|
4.8
|
26.8
|
1.0
|
HG23
|
E:ILE165
|
4.9
|
23.4
|
1.0
|
CG
|
F:ASN112
|
4.9
|
36.7
|
1.0
|
H11
|
E:CAP500
|
4.9
|
30.6
|
1.0
|
CD2
|
E:HIS288
|
4.9
|
33.0
|
1.0
|
HD13
|
E:ILE165
|
4.9
|
17.1
|
1.0
|
H51
|
E:CAP500
|
4.9
|
29.5
|
1.0
|
HG2
|
E:GLU195
|
4.9
|
35.8
|
1.0
|
HB2
|
E:ASP194
|
4.9
|
30.4
|
1.0
|
C5
|
E:CAP500
|
5.0
|
31.1
|
1.0
|
|
Magnesium binding site 6 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 6 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg501
b:32.1
occ:1.00
|
HO3
|
F:CAP500
|
1.5
|
40.7
|
1.0
|
OD1
|
F:ASP194
|
2.0
|
37.5
|
1.0
|
OE1
|
F:GLU195
|
2.0
|
30.7
|
1.0
|
OQ2
|
F:KCX192
|
2.0
|
25.8
|
1.0
|
O2
|
F:CAP500
|
2.1
|
36.4
|
1.0
|
O6
|
F:CAP500
|
2.1
|
27.0
|
1.0
|
O3
|
F:CAP500
|
2.3
|
39.5
|
1.0
|
HO2
|
F:CAP500
|
2.7
|
35.5
|
1.0
|
C2
|
F:CAP500
|
2.7
|
34.0
|
1.0
|
C
|
F:CAP500
|
2.8
|
34.1
|
1.0
|
H
|
F:GLU195
|
2.8
|
33.5
|
1.0
|
HD21
|
E:ASN112
|
2.9
|
32.2
|
1.0
|
C3
|
F:CAP500
|
3.0
|
33.9
|
1.0
|
CX
|
F:KCX192
|
3.1
|
29.8
|
1.0
|
HZ2
|
F:LYS167
|
3.1
|
26.1
|
1.0
|
CD
|
F:GLU195
|
3.1
|
33.7
|
1.0
|
CG
|
F:ASP194
|
3.1
|
34.1
|
1.0
|
HG21
|
F:ILE165
|
3.3
|
28.5
|
1.0
|
OQ1
|
F:KCX192
|
3.3
|
33.6
|
1.0
|
HE2
|
F:HIS288
|
3.4
|
31.6
|
1.0
|
H3
|
F:CAP500
|
3.4
|
33.2
|
1.0
|
HZ3
|
F:LYS169
|
3.4
|
39.4
|
1.0
|
HZ2
|
F:LYS169
|
3.5
|
35.5
|
1.0
|
HA
|
F:ASP194
|
3.5
|
26.1
|
1.0
|
ND2
|
E:ASN112
|
3.7
|
30.8
|
1.0
|
HD22
|
E:ASN112
|
3.7
|
30.5
|
1.0
|
OE2
|
F:GLU195
|
3.7
|
33.9
|
1.0
|
HZ1
|
F:LYS169
|
3.7
|
39.2
|
1.0
|
NZ
|
F:LYS169
|
3.7
|
37.8
|
1.0
|
OD2
|
F:ASP194
|
3.8
|
38.8
|
1.0
|
N
|
F:GLU195
|
3.8
|
32.6
|
1.0
|
NZ
|
F:LYS167
|
3.9
|
28.4
|
1.0
|
HB3
|
F:GLU195
|
3.9
|
37.0
|
1.0
|
NE2
|
F:HIS288
|
4.0
|
31.8
|
1.0
|
O7
|
F:CAP500
|
4.0
|
36.3
|
1.0
|
HZ1
|
F:LYS167
|
4.0
|
30.2
|
1.0
|
HZ3
|
F:LYS167
|
4.1
|
28.9
|
1.0
|
C1
|
F:CAP500
|
4.2
|
33.0
|
1.0
|
CA
|
F:ASP194
|
4.2
|
25.9
|
1.0
|
CB
|
F:ASP194
|
4.2
|
27.6
|
1.0
|
HE1
|
F:HIS288
|
4.3
|
32.8
|
1.0
|
NZ
|
F:KCX192
|
4.3
|
32.1
|
1.0
|
HG12
|
F:ILE165
|
4.3
|
31.9
|
1.0
|
CG
|
F:GLU195
|
4.3
|
33.1
|
1.0
|
C4
|
F:CAP500
|
4.3
|
41.0
|
1.0
|
CG2
|
F:ILE165
|
4.4
|
27.9
|
1.0
|
HD3
|
F:PRO196
|
4.4
|
35.1
|
1.0
|
CE1
|
F:HIS288
|
4.4
|
32.3
|
1.0
|
CB
|
F:GLU195
|
4.5
|
36.0
|
1.0
|
C
|
F:ASP194
|
4.5
|
31.1
|
1.0
|
H4
|
F:CAP500
|
4.5
|
41.8
|
1.0
|
H11
|
F:CAP500
|
4.6
|
32.3
|
1.0
|
O1
|
F:CAP500
|
4.6
|
30.2
|
1.0
|
H52
|
F:CAP500
|
4.7
|
43.0
|
1.0
|
HG22
|
F:ILE165
|
4.7
|
27.1
|
1.0
|
CA
|
F:GLU195
|
4.8
|
33.9
|
1.0
|
H12
|
F:CAP500
|
4.8
|
33.4
|
1.0
|
HG3
|
F:LYS169
|
4.8
|
39.8
|
1.0
|
HB3
|
F:ASP194
|
4.8
|
29.0
|
1.0
|
HG23
|
F:ILE165
|
4.9
|
27.5
|
1.0
|
HG3
|
F:GLU195
|
4.9
|
34.3
|
1.0
|
HD13
|
F:ILE165
|
4.9
|
24.8
|
1.0
|
O
|
F:HOH728
|
4.9
|
39.4
|
1.0
|
CG
|
E:ASN112
|
4.9
|
38.2
|
1.0
|
H51
|
F:CAP500
|
4.9
|
41.6
|
1.0
|
C5
|
F:CAP500
|
4.9
|
41.4
|
1.0
|
CD2
|
F:HIS288
|
5.0
|
33.5
|
1.0
|
O
|
E:HOH725
|
5.0
|
35.0
|
1.0
|
HB2
|
F:ASP194
|
5.0
|
28.7
|
1.0
|
|
Magnesium binding site 7 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 7 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg501
b:33.2
occ:1.00
|
HO3
|
G:CAP500
|
1.4
|
36.7
|
1.0
|
OE1
|
G:GLU195
|
1.9
|
29.0
|
1.0
|
OQ2
|
G:KCX192
|
2.0
|
34.0
|
1.0
|
OD1
|
G:ASP194
|
2.0
|
33.0
|
1.0
|
O2
|
G:CAP500
|
2.2
|
36.2
|
1.0
|
O6
|
G:CAP500
|
2.2
|
35.1
|
1.0
|
O3
|
G:CAP500
|
2.2
|
37.0
|
1.0
|
HO2
|
G:CAP500
|
2.7
|
36.3
|
1.0
|
C2
|
G:CAP500
|
2.8
|
37.3
|
1.0
|
H
|
G:GLU195
|
2.8
|
36.7
|
1.0
|
C
|
G:CAP500
|
2.8
|
38.7
|
1.0
|
HD22
|
H:ASN112
|
3.0
|
40.2
|
1.0
|
C3
|
G:CAP500
|
3.0
|
36.8
|
1.0
|
CX
|
G:KCX192
|
3.1
|
35.7
|
1.0
|
CD
|
G:GLU195
|
3.1
|
45.8
|
1.0
|
HZ2
|
G:LYS167
|
3.2
|
40.7
|
1.0
|
CG
|
G:ASP194
|
3.2
|
37.3
|
1.0
|
OQ1
|
G:KCX192
|
3.3
|
34.0
|
1.0
|
HE2
|
G:HIS288
|
3.3
|
34.0
|
1.0
|
H3
|
G:CAP500
|
3.4
|
34.7
|
1.0
|
HG21
|
G:ILE165
|
3.4
|
31.9
|
1.0
|
HZ2
|
G:LYS169
|
3.5
|
48.7
|
1.0
|
HZ3
|
G:LYS169
|
3.5
|
49.9
|
1.0
|
HA
|
G:ASP194
|
3.5
|
37.8
|
1.0
|
HD21
|
H:ASN112
|
3.7
|
40.9
|
1.0
|
ND2
|
H:ASN112
|
3.7
|
39.9
|
1.0
|
OE2
|
G:GLU195
|
3.7
|
42.7
|
1.0
|
HZ1
|
G:LYS169
|
3.8
|
50.3
|
1.0
|
NZ
|
G:LYS169
|
3.8
|
49.8
|
1.0
|
N
|
G:GLU195
|
3.8
|
36.8
|
1.0
|
HB3
|
G:GLU195
|
3.9
|
38.3
|
1.0
|
OD2
|
G:ASP194
|
3.9
|
37.4
|
1.0
|
NE2
|
G:HIS288
|
3.9
|
34.2
|
1.0
|
NZ
|
G:LYS167
|
4.0
|
40.9
|
1.0
|
O7
|
G:CAP500
|
4.0
|
40.3
|
1.0
|
HZ1
|
G:LYS167
|
4.1
|
41.9
|
1.0
|
HE1
|
G:HIS288
|
4.2
|
34.8
|
1.0
|
C1
|
G:CAP500
|
4.2
|
37.3
|
1.0
|
HZ3
|
G:LYS167
|
4.2
|
40.9
|
1.0
|
CA
|
G:ASP194
|
4.2
|
34.9
|
1.0
|
CG
|
G:GLU195
|
4.2
|
42.6
|
1.0
|
NZ
|
G:KCX192
|
4.3
|
34.8
|
1.0
|
C4
|
G:CAP500
|
4.3
|
39.8
|
1.0
|
CB
|
G:ASP194
|
4.3
|
34.8
|
1.0
|
HG12
|
G:ILE165
|
4.3
|
28.3
|
1.0
|
CE1
|
G:HIS288
|
4.4
|
33.6
|
1.0
|
HD3
|
G:PRO196
|
4.4
|
38.0
|
1.0
|
CB
|
G:GLU195
|
4.4
|
37.7
|
1.0
|
CG2
|
G:ILE165
|
4.4
|
33.1
|
1.0
|
H4
|
G:CAP500
|
4.5
|
39.3
|
1.0
|
C
|
G:ASP194
|
4.5
|
40.4
|
1.0
|
H12
|
G:CAP500
|
4.6
|
38.3
|
1.0
|
H52
|
G:CAP500
|
4.6
|
39.7
|
1.0
|
O1
|
G:CAP500
|
4.6
|
32.3
|
1.0
|
CA
|
G:GLU195
|
4.7
|
36.8
|
1.0
|
HG22
|
G:ILE165
|
4.8
|
34.6
|
1.0
|
HG3
|
G:GLU195
|
4.8
|
42.9
|
1.0
|
H11
|
G:CAP500
|
4.8
|
37.3
|
1.0
|
H51
|
G:CAP500
|
4.8
|
39.4
|
1.0
|
C5
|
G:CAP500
|
4.8
|
39.7
|
1.0
|
CG
|
H:ASN112
|
4.8
|
37.9
|
1.0
|
HG3
|
G:LYS169
|
4.9
|
32.5
|
1.0
|
O
|
H:HOH715
|
4.9
|
42.4
|
1.0
|
CD2
|
G:HIS288
|
4.9
|
35.2
|
1.0
|
HB3
|
G:ASP194
|
4.9
|
35.5
|
1.0
|
HD13
|
G:ILE165
|
4.9
|
39.5
|
1.0
|
HG23
|
G:ILE165
|
4.9
|
30.8
|
1.0
|
HG2
|
G:GLU195
|
5.0
|
44.0
|
1.0
|
|
Magnesium binding site 8 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 8 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg501
b:33.0
occ:1.00
|
HO3
|
H:CAP500
|
1.5
|
36.5
|
1.0
|
OE1
|
H:GLU195
|
1.9
|
36.0
|
1.0
|
OQ2
|
H:KCX192
|
1.9
|
28.2
|
1.0
|
OD1
|
H:ASP194
|
1.9
|
33.1
|
1.0
|
O2
|
H:CAP500
|
2.2
|
39.4
|
1.0
|
O6
|
H:CAP500
|
2.2
|
31.0
|
1.0
|
O3
|
H:CAP500
|
2.3
|
36.2
|
1.0
|
H
|
H:GLU195
|
2.7
|
31.6
|
1.0
|
HO2
|
H:CAP500
|
2.7
|
41.0
|
1.0
|
C2
|
H:CAP500
|
2.9
|
34.6
|
1.0
|
C
|
H:CAP500
|
2.9
|
31.1
|
1.0
|
HD21
|
G:ASN112
|
3.0
|
41.7
|
1.0
|
CX
|
H:KCX192
|
3.0
|
31.0
|
1.0
|
CD
|
H:GLU195
|
3.0
|
46.4
|
1.0
|
C3
|
H:CAP500
|
3.1
|
32.8
|
1.0
|
CG
|
H:ASP194
|
3.1
|
34.9
|
1.0
|
HZ2
|
H:LYS167
|
3.2
|
36.1
|
1.0
|
OQ1
|
H:KCX192
|
3.3
|
33.9
|
1.0
|
HG21
|
H:ILE165
|
3.4
|
30.5
|
1.0
|
HA
|
H:ASP194
|
3.4
|
33.2
|
1.0
|
HZ3
|
H:LYS169
|
3.5
|
42.0
|
1.0
|
H3
|
H:CAP500
|
3.5
|
33.3
|
1.0
|
HZ2
|
H:LYS169
|
3.5
|
41.5
|
1.0
|
OE2
|
H:GLU195
|
3.6
|
38.1
|
1.0
|
N
|
H:GLU195
|
3.7
|
32.0
|
1.0
|
ND2
|
G:ASN112
|
3.7
|
42.1
|
1.0
|
HD22
|
G:ASN112
|
3.7
|
42.6
|
1.0
|
NZ
|
H:LYS169
|
3.8
|
41.8
|
1.0
|
HZ1
|
H:LYS169
|
3.8
|
42.4
|
1.0
|
OD2
|
H:ASP194
|
3.8
|
40.8
|
1.0
|
HB3
|
H:GLU195
|
3.8
|
34.4
|
1.0
|
NE2
|
H:HIS288
|
3.9
|
39.0
|
1.0
|
NZ
|
H:LYS167
|
4.0
|
37.1
|
1.0
|
O7
|
H:CAP500
|
4.1
|
28.3
|
1.0
|
HZ1
|
H:LYS167
|
4.1
|
37.9
|
1.0
|
CA
|
H:ASP194
|
4.1
|
31.3
|
1.0
|
HG12
|
H:ILE165
|
4.1
|
31.2
|
1.0
|
NZ
|
H:KCX192
|
4.2
|
31.9
|
1.0
|
CB
|
H:ASP194
|
4.2
|
32.9
|
1.0
|
CG
|
H:GLU195
|
4.2
|
32.9
|
1.0
|
HE1
|
H:HIS288
|
4.2
|
38.1
|
1.0
|
HZ3
|
H:LYS167
|
4.3
|
38.2
|
1.0
|
C1
|
H:CAP500
|
4.3
|
34.7
|
1.0
|
HD3
|
H:PRO196
|
4.3
|
34.9
|
1.0
|
CB
|
H:GLU195
|
4.4
|
34.7
|
1.0
|
C
|
H:ASP194
|
4.4
|
33.8
|
1.0
|
C4
|
H:CAP500
|
4.4
|
33.1
|
1.0
|
CE1
|
H:HIS288
|
4.4
|
37.5
|
1.0
|
CG2
|
H:ILE165
|
4.5
|
30.9
|
1.0
|
H4
|
H:CAP500
|
4.6
|
32.0
|
1.0
|
H12
|
H:CAP500
|
4.6
|
34.2
|
1.0
|
CA
|
H:GLU195
|
4.6
|
33.3
|
1.0
|
O1
|
H:CAP500
|
4.7
|
36.2
|
1.0
|
H52
|
H:CAP500
|
4.7
|
31.9
|
1.0
|
HG3
|
H:LYS169
|
4.8
|
47.6
|
1.0
|
HB3
|
H:ASP194
|
4.8
|
33.5
|
1.0
|
HG3
|
H:GLU195
|
4.8
|
32.3
|
1.0
|
HG23
|
H:ILE165
|
4.9
|
28.9
|
1.0
|
HG22
|
H:ILE165
|
4.9
|
31.0
|
1.0
|
H11
|
H:CAP500
|
4.9
|
35.8
|
1.0
|
CD2
|
H:HIS288
|
4.9
|
39.3
|
1.0
|
HB2
|
H:ASP194
|
4.9
|
32.9
|
1.0
|
HG2
|
H:GLU195
|
4.9
|
33.9
|
1.0
|
H51
|
H:CAP500
|
5.0
|
32.1
|
1.0
|
CG
|
G:ASN112
|
5.0
|
37.8
|
1.0
|
C5
|
H:CAP500
|
5.0
|
31.5
|
1.0
|
O
|
G:HOH718
|
5.0
|
42.7
|
1.0
|
|
Magnesium binding site 9 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 9 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Mg501
b:42.3
occ:1.00
|
HO3
|
I:CAP500
|
1.4
|
42.1
|
1.0
|
OE1
|
I:GLU195
|
1.9
|
31.0
|
1.0
|
OQ2
|
I:KCX192
|
2.0
|
38.6
|
1.0
|
OD1
|
I:ASP194
|
2.0
|
37.7
|
1.0
|
O2
|
I:CAP500
|
2.2
|
41.7
|
1.0
|
O3
|
I:CAP500
|
2.2
|
42.2
|
1.0
|
O6
|
I:CAP500
|
2.2
|
34.4
|
1.0
|
HO2
|
I:CAP500
|
2.7
|
41.0
|
1.0
|
H
|
I:GLU195
|
2.8
|
29.2
|
1.0
|
C2
|
I:CAP500
|
2.8
|
41.1
|
1.0
|
C
|
I:CAP500
|
2.8
|
40.6
|
1.0
|
HD21
|
J:ASN112
|
2.9
|
31.9
|
1.0
|
C3
|
I:CAP500
|
3.0
|
39.9
|
1.0
|
CX
|
I:KCX192
|
3.1
|
35.6
|
1.0
|
CD
|
I:GLU195
|
3.1
|
48.4
|
1.0
|
HZ2
|
I:LYS167
|
3.2
|
37.7
|
1.0
|
CG
|
I:ASP194
|
3.2
|
37.6
|
1.0
|
OQ1
|
I:KCX192
|
3.3
|
33.7
|
1.0
|
HE2
|
I:HIS288
|
3.3
|
41.5
|
1.0
|
H3
|
I:CAP500
|
3.4
|
39.4
|
1.0
|
HG21
|
I:ILE165
|
3.4
|
37.4
|
1.0
|
HZ2
|
I:LYS169
|
3.5
|
34.1
|
1.0
|
HZ3
|
I:LYS169
|
3.5
|
34.5
|
1.0
|
HA
|
I:ASP194
|
3.5
|
35.9
|
1.0
|
ND2
|
J:ASN112
|
3.6
|
30.4
|
1.0
|
OE2
|
I:GLU195
|
3.7
|
45.4
|
1.0
|
HD22
|
J:ASN112
|
3.7
|
28.7
|
1.0
|
N
|
I:GLU195
|
3.8
|
31.2
|
1.0
|
HZ1
|
I:LYS169
|
3.8
|
36.0
|
1.0
|
NZ
|
I:LYS169
|
3.8
|
35.2
|
1.0
|
HB3
|
I:GLU195
|
3.8
|
33.4
|
1.0
|
NE2
|
I:HIS288
|
3.9
|
39.8
|
1.0
|
OD2
|
I:ASP194
|
3.9
|
42.4
|
1.0
|
NZ
|
I:LYS167
|
4.0
|
38.9
|
1.0
|
O7
|
I:CAP500
|
4.0
|
42.3
|
1.0
|
HE1
|
I:HIS288
|
4.1
|
38.9
|
1.0
|
HZ1
|
I:LYS167
|
4.2
|
39.4
|
1.0
|
CG
|
I:GLU195
|
4.2
|
41.7
|
1.0
|
C1
|
I:CAP500
|
4.2
|
42.5
|
1.0
|
NZ
|
I:KCX192
|
4.2
|
36.2
|
1.0
|
HZ3
|
I:LYS167
|
4.2
|
40.0
|
1.0
|
CA
|
I:ASP194
|
4.2
|
34.2
|
1.0
|
C4
|
I:CAP500
|
4.3
|
40.8
|
1.0
|
CB
|
I:ASP194
|
4.3
|
35.6
|
1.0
|
CE1
|
I:HIS288
|
4.3
|
39.0
|
1.0
|
HG12
|
I:ILE165
|
4.3
|
37.4
|
1.0
|
HD3
|
I:PRO196
|
4.4
|
37.6
|
1.0
|
CB
|
I:GLU195
|
4.4
|
32.3
|
1.0
|
CG2
|
I:ILE165
|
4.5
|
36.6
|
1.0
|
C
|
I:ASP194
|
4.5
|
34.8
|
1.0
|
H4
|
I:CAP500
|
4.5
|
41.3
|
1.0
|
H52
|
I:CAP500
|
4.6
|
41.1
|
1.0
|
H11
|
I:CAP500
|
4.6
|
41.5
|
1.0
|
O1
|
I:CAP500
|
4.7
|
41.4
|
1.0
|
CA
|
I:GLU195
|
4.7
|
32.2
|
1.0
|
HG3
|
I:GLU195
|
4.8
|
40.1
|
1.0
|
HG22
|
I:ILE165
|
4.8
|
36.6
|
1.0
|
H12
|
I:CAP500
|
4.8
|
43.3
|
1.0
|
CG
|
J:ASN112
|
4.8
|
37.1
|
1.0
|
H51
|
I:CAP500
|
4.8
|
40.1
|
1.0
|
C5
|
I:CAP500
|
4.9
|
40.2
|
1.0
|
CD2
|
I:HIS288
|
4.9
|
39.4
|
1.0
|
HG3
|
I:LYS169
|
4.9
|
38.2
|
1.0
|
HB3
|
I:ASP194
|
4.9
|
35.8
|
1.0
|
HG23
|
I:ILE165
|
4.9
|
35.1
|
1.0
|
HD13
|
I:ILE165
|
4.9
|
29.6
|
1.0
|
HG2
|
I:GLU195
|
5.0
|
41.1
|
1.0
|
O
|
J:HOH612
|
5.0
|
48.2
|
1.0
|
|
Magnesium binding site 10 out
of 12 in 5han
Go back to
Magnesium Binding Sites List in 5han
Magnesium binding site 10 out
of 12 in the Structure Function Studies of R. Palustris Rubisco (S59F 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 Mutant; Cabp- Bound) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Mg501
b:35.0
occ:1.00
|
HO3
|
J:CAP500
|
1.4
|
42.3
|
1.0
|
OE1
|
J:GLU195
|
1.9
|
39.6
|
1.0
|
OQ2
|
J:KCX192
|
2.0
|
31.1
|
1.0
|
OD1
|
J:ASP194
|
2.0
|
46.7
|
1.0
|
O2
|
J:CAP500
|
2.2
|
43.2
|
1.0
|
O6
|
J:CAP500
|
2.2
|
42.4
|
1.0
|
O3
|
J:CAP500
|
2.2
|
43.5
|
1.0
|
HO2
|
J:CAP500
|
2.7
|
42.6
|
1.0
|
H
|
J:GLU195
|
2.8
|
32.2
|
1.0
|
C2
|
J:CAP500
|
2.8
|
43.5
|
1.0
|
C
|
J:CAP500
|
2.8
|
41.4
|
1.0
|
HD21
|
I:ASN112
|
2.9
|
40.6
|
1.0
|
C3
|
J:CAP500
|
3.0
|
44.6
|
1.0
|
CX
|
J:KCX192
|
3.0
|
34.0
|
1.0
|
CD
|
J:GLU195
|
3.1
|
44.8
|
1.0
|
HZ2
|
J:LYS167
|
3.2
|
33.0
|
1.0
|
CG
|
J:ASP194
|
3.2
|
42.4
|
1.0
|
OQ1
|
J:KCX192
|
3.3
|
37.9
|
1.0
|
HG21
|
J:ILE165
|
3.4
|
30.8
|
1.0
|
H3
|
J:CAP500
|
3.4
|
45.2
|
1.0
|
HZ2
|
J:LYS169
|
3.5
|
44.0
|
1.0
|
HZ3
|
J:LYS169
|
3.5
|
45.1
|
1.0
|
HA
|
J:ASP194
|
3.5
|
23.5
|
1.0
|
OE2
|
J:GLU195
|
3.6
|
40.6
|
1.0
|
ND2
|
I:ASN112
|
3.7
|
40.7
|
1.0
|
HD22
|
I:ASN112
|
3.7
|
40.3
|
1.0
|
N
|
J:GLU195
|
3.8
|
31.6
|
1.0
|
NZ
|
J:LYS169
|
3.8
|
45.3
|
1.0
|
HZ1
|
J:LYS169
|
3.8
|
46.1
|
1.0
|
HB3
|
J:GLU195
|
3.8
|
31.5
|
1.0
|
OD2
|
J:ASP194
|
3.8
|
47.8
|
1.0
|
NE2
|
J:HIS288
|
3.9
|
37.5
|
1.0
|
NZ
|
J:LYS167
|
4.0
|
31.9
|
1.0
|
O7
|
J:CAP500
|
4.1
|
45.0
|
1.0
|
HZ1
|
J:LYS167
|
4.1
|
32.1
|
1.0
|
HE1
|
J:HIS288
|
4.2
|
37.1
|
1.0
|
CA
|
J:ASP194
|
4.2
|
28.6
|
1.0
|
NZ
|
J:KCX192
|
4.2
|
32.1
|
1.0
|
CG
|
J:GLU195
|
4.2
|
44.3
|
1.0
|
HZ3
|
J:LYS167
|
4.2
|
31.2
|
1.0
|
C1
|
J:CAP500
|
4.3
|
44.2
|
1.0
|
CB
|
J:ASP194
|
4.3
|
30.2
|
1.0
|
HG12
|
J:ILE165
|
4.3
|
34.7
|
1.0
|
HD3
|
J:PRO196
|
4.3
|
37.4
|
1.0
|
C4
|
J:CAP500
|
4.4
|
43.4
|
1.0
|
CE1
|
J:HIS288
|
4.4
|
36.3
|
1.0
|
CB
|
J:GLU195
|
4.4
|
31.7
|
1.0
|
CG2
|
J:ILE165
|
4.4
|
30.9
|
1.0
|
C
|
J:ASP194
|
4.5
|
35.2
|
1.0
|
H4
|
J:CAP500
|
4.6
|
42.8
|
1.0
|
H12
|
J:CAP500
|
4.6
|
44.1
|
1.0
|
H52
|
J:CAP500
|
4.6
|
38.7
|
1.0
|
O1
|
J:CAP500
|
4.7
|
41.6
|
1.0
|
CA
|
J:GLU195
|
4.7
|
30.7
|
1.0
|
HG22
|
J:ILE165
|
4.8
|
31.4
|
1.0
|
HG3
|
J:GLU195
|
4.8
|
44.7
|
1.0
|
HG3
|
J:LYS169
|
4.8
|
32.8
|
1.0
|
HB3
|
J:ASP194
|
4.9
|
31.4
|
1.0
|
H11
|
J:CAP500
|
4.9
|
44.8
|
1.0
|
CD2
|
J:HIS288
|
4.9
|
37.4
|
1.0
|
H51
|
J:CAP500
|
4.9
|
39.5
|
1.0
|
HG23
|
J:ILE165
|
4.9
|
29.2
|
1.0
|
CG
|
I:ASN112
|
4.9
|
45.5
|
1.0
|
C5
|
J:CAP500
|
4.9
|
39.8
|
1.0
|
HD13
|
J:ILE165
|
4.9
|
35.3
|
1.0
|
HG2
|
J:GLU195
|
5.0
|
43.3
|
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 15:44:55 2024
|