Magnesium in PDB 1uwa: L290F Mutant Rubisco From Chlamydomonas
Enzymatic activity of L290F Mutant Rubisco From Chlamydomonas
All present enzymatic activity of L290F Mutant Rubisco From Chlamydomonas:
4.1.1.39;
Protein crystallography data
The structure of L290F Mutant Rubisco From Chlamydomonas, PDB code: 1uwa
was solved by
S.Karkehabadi,
T.C.Taylor,
R.J.Spreitzer,
I.Andersson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
30.00 /
2.30
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
120.983,
177.709,
122.663,
90.00,
117.70,
90.00
|
|
R / Rfree (%)
|
17.1 /
20.5
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the L290F Mutant Rubisco From Chlamydomonas
(pdb code 1uwa). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
L290F Mutant Rubisco From Chlamydomonas, PDB code: 1uwa:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 1uwa
Go back to
Magnesium Binding Sites List in 1uwa
Magnesium binding site 1 out
of 8 in the L290F Mutant Rubisco From Chlamydomonas
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of L290F Mutant Rubisco From Chlamydomonas within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg501
b:27.2
occ:1.00
|
OD1
|
A:ASP203
|
1.9
|
30.7
|
1.0
|
|
OQ2
|
A:KCX201
|
2.0
|
23.7
|
1.0
|
|
OE1
|
A:GLU204
|
2.1
|
30.5
|
1.0
|
|
O3
|
A:CAP502
|
2.1
|
32.2
|
1.0
|
|
O7
|
A:CAP502
|
2.2
|
32.4
|
1.0
|
|
O2
|
A:CAP502
|
2.2
|
32.9
|
1.0
|
|
C2
|
A:CAP502
|
2.8
|
32.7
|
1.0
|
|
C
|
A:CAP502
|
2.9
|
32.8
|
1.0
|
|
C3
|
A:CAP502
|
3.0
|
31.9
|
1.0
|
|
CX
|
A:KCX201
|
3.0
|
27.6
|
1.0
|
|
CG
|
A:ASP203
|
3.1
|
30.5
|
1.0
|
|
CD
|
A:GLU204
|
3.2
|
31.7
|
1.0
|
|
OQ1
|
A:KCX201
|
3.3
|
29.7
|
1.0
|
|
OE2
|
A:GLU204
|
3.6
|
33.2
|
1.0
|
|
NZ
|
A:LYS177
|
3.7
|
30.0
|
1.0
|
|
OD2
|
A:ASP203
|
3.8
|
34.7
|
1.0
|
|
N
|
A:GLU204
|
3.8
|
26.9
|
1.0
|
|
NZ
|
A:LYS175
|
3.9
|
28.3
|
1.0
|
|
ND2
|
O:ASN123
|
3.9
|
31.1
|
1.0
|
|
CG2
|
A:THR173
|
4.0
|
27.9
|
1.0
|
|
NE2
|
A:HIS294
|
4.1
|
25.2
|
1.0
|
|
CA
|
A:ASP203
|
4.1
|
26.6
|
1.0
|
|
CB
|
A:ASP203
|
4.2
|
26.7
|
1.0
|
|
O6
|
A:CAP502
|
4.2
|
32.9
|
1.0
|
|
NZ
|
A:KCX201
|
4.2
|
25.9
|
1.0
|
|
C4
|
A:CAP502
|
4.2
|
34.0
|
1.0
|
|
C1
|
A:CAP502
|
4.3
|
32.1
|
1.0
|
|
OG1
|
A:THR173
|
4.3
|
34.0
|
1.0
|
|
CG
|
A:GLU204
|
4.4
|
25.6
|
1.0
|
|
C
|
A:ASP203
|
4.5
|
27.6
|
1.0
|
|
CB
|
A:GLU204
|
4.6
|
27.5
|
1.0
|
|
CD2
|
A:HIS294
|
4.7
|
21.6
|
1.0
|
|
CB
|
A:THR173
|
4.7
|
31.6
|
1.0
|
|
C5
|
A:CAP502
|
4.8
|
30.7
|
1.0
|
|
O1
|
A:CAP502
|
4.8
|
31.1
|
1.0
|
|
CA
|
A:GLU204
|
4.8
|
27.1
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 1uwa
Go back to
Magnesium Binding Sites List in 1uwa
Magnesium binding site 2 out
of 8 in the L290F Mutant Rubisco From Chlamydomonas
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of L290F Mutant Rubisco From Chlamydomonas within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg501
b:27.6
occ:1.00
|
OD1
|
B:ASP203
|
1.9
|
30.9
|
1.0
|
|
OE1
|
B:GLU204
|
2.1
|
30.5
|
1.0
|
|
O7
|
B:CAP502
|
2.1
|
32.2
|
1.0
|
|
OQ2
|
B:KCX201
|
2.1
|
24.0
|
1.0
|
|
O3
|
B:CAP502
|
2.1
|
32.2
|
1.0
|
|
O2
|
B:CAP502
|
2.2
|
32.7
|
1.0
|
|
C2
|
B:CAP502
|
2.8
|
32.6
|
1.0
|
|
C
|
B:CAP502
|
2.9
|
32.6
|
1.0
|
|
C3
|
B:CAP502
|
3.0
|
32.0
|
1.0
|
|
CX
|
B:KCX201
|
3.1
|
27.4
|
1.0
|
|
CD
|
B:GLU204
|
3.2
|
31.7
|
1.0
|
|
CG
|
B:ASP203
|
3.2
|
30.7
|
1.0
|
|
OQ1
|
B:KCX201
|
3.3
|
29.7
|
1.0
|
|
OE2
|
B:GLU204
|
3.6
|
33.0
|
1.0
|
|
NZ
|
B:LYS177
|
3.7
|
30.2
|
1.0
|
|
OD2
|
B:ASP203
|
3.8
|
34.5
|
1.0
|
|
N
|
B:GLU204
|
3.8
|
27.1
|
1.0
|
|
ND2
|
E:ASN123
|
3.9
|
31.0
|
1.0
|
|
NZ
|
B:LYS175
|
4.0
|
27.9
|
1.0
|
|
CG2
|
B:THR173
|
4.0
|
28.1
|
1.0
|
|
NE2
|
B:HIS294
|
4.1
|
24.9
|
1.0
|
|
O6
|
B:CAP502
|
4.1
|
32.8
|
1.0
|
|
CA
|
B:ASP203
|
4.1
|
26.7
|
1.0
|
|
CB
|
B:ASP203
|
4.2
|
26.6
|
1.0
|
|
C4
|
B:CAP502
|
4.2
|
33.9
|
1.0
|
|
NZ
|
B:KCX201
|
4.2
|
25.4
|
1.0
|
|
C1
|
B:CAP502
|
4.3
|
32.1
|
1.0
|
|
OG1
|
B:THR173
|
4.4
|
33.8
|
1.0
|
|
CG
|
B:GLU204
|
4.4
|
25.6
|
1.0
|
|
C
|
B:ASP203
|
4.5
|
27.4
|
1.0
|
|
CB
|
B:GLU204
|
4.5
|
27.4
|
1.0
|
|
CD2
|
B:HIS294
|
4.7
|
21.6
|
1.0
|
|
CB
|
B:THR173
|
4.7
|
31.7
|
1.0
|
|
C5
|
B:CAP502
|
4.7
|
30.6
|
1.0
|
|
CA
|
B:GLU204
|
4.8
|
27.1
|
1.0
|
|
O1
|
B:CAP502
|
4.8
|
30.7
|
1.0
|
|
CE1
|
B:HIS294
|
5.0
|
24.8
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 1uwa
Go back to
Magnesium Binding Sites List in 1uwa
Magnesium binding site 3 out
of 8 in the L290F Mutant Rubisco From Chlamydomonas
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of L290F Mutant Rubisco From Chlamydomonas within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg501
b:27.1
occ:1.00
|
OQ2
|
E:KCX201
|
2.0
|
24.1
|
1.0
|
|
OD1
|
E:ASP203
|
2.0
|
30.9
|
1.0
|
|
O3
|
E:CAP502
|
2.1
|
32.5
|
1.0
|
|
OE1
|
E:GLU204
|
2.1
|
30.6
|
1.0
|
|
O7
|
E:CAP502
|
2.1
|
32.2
|
1.0
|
|
O2
|
E:CAP502
|
2.2
|
32.9
|
1.0
|
|
C2
|
E:CAP502
|
2.8
|
32.6
|
1.0
|
|
C
|
E:CAP502
|
2.9
|
32.9
|
1.0
|
|
C3
|
E:CAP502
|
3.0
|
31.8
|
1.0
|
|
CX
|
E:KCX201
|
3.0
|
27.5
|
1.0
|
|
CD
|
E:GLU204
|
3.2
|
31.4
|
1.0
|
|
CG
|
E:ASP203
|
3.2
|
30.9
|
1.0
|
|
OQ1
|
E:KCX201
|
3.3
|
29.8
|
1.0
|
|
OE2
|
E:GLU204
|
3.6
|
32.4
|
1.0
|
|
NZ
|
E:LYS177
|
3.7
|
30.2
|
1.0
|
|
N
|
E:GLU204
|
3.8
|
26.8
|
1.0
|
|
OD2
|
E:ASP203
|
3.9
|
34.5
|
1.0
|
|
ND2
|
B:ASN123
|
3.9
|
31.0
|
1.0
|
|
NZ
|
E:LYS175
|
3.9
|
28.1
|
1.0
|
|
CG2
|
E:THR173
|
4.0
|
27.8
|
1.0
|
|
NE2
|
E:HIS294
|
4.0
|
25.0
|
1.0
|
|
CA
|
E:ASP203
|
4.1
|
26.5
|
1.0
|
|
O6
|
E:CAP502
|
4.1
|
33.3
|
1.0
|
|
NZ
|
E:KCX201
|
4.2
|
26.1
|
1.0
|
|
C4
|
E:CAP502
|
4.2
|
34.0
|
1.0
|
|
CB
|
E:ASP203
|
4.2
|
26.5
|
1.0
|
|
C1
|
E:CAP502
|
4.3
|
31.9
|
1.0
|
|
OG1
|
E:THR173
|
4.3
|
34.4
|
1.0
|
|
CG
|
E:GLU204
|
4.4
|
25.8
|
1.0
|
|
C
|
E:ASP203
|
4.5
|
27.4
|
1.0
|
|
CB
|
E:GLU204
|
4.6
|
27.4
|
1.0
|
|
CD2
|
E:HIS294
|
4.6
|
21.7
|
1.0
|
|
C5
|
E:CAP502
|
4.7
|
30.5
|
1.0
|
|
CB
|
E:THR173
|
4.7
|
31.8
|
1.0
|
|
O1
|
E:CAP502
|
4.8
|
30.8
|
1.0
|
|
CA
|
E:GLU204
|
4.8
|
27.3
|
1.0
|
|
CE1
|
E:HIS294
|
5.0
|
25.1
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 1uwa
Go back to
Magnesium Binding Sites List in 1uwa
Magnesium binding site 4 out
of 8 in the L290F Mutant Rubisco From Chlamydomonas
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of L290F Mutant Rubisco From Chlamydomonas within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg501
b:28.2
occ:1.00
|
OQ2
|
H:KCX201
|
1.9
|
23.9
|
1.0
|
|
OD1
|
H:ASP203
|
1.9
|
30.8
|
1.0
|
|
OE1
|
H:GLU204
|
2.0
|
30.5
|
1.0
|
|
O3
|
H:CAP502
|
2.1
|
32.3
|
1.0
|
|
O2
|
H:CAP502
|
2.2
|
32.9
|
1.0
|
|
O7
|
H:CAP502
|
2.2
|
32.4
|
1.0
|
|
C2
|
H:CAP502
|
2.9
|
32.8
|
1.0
|
|
C
|
H:CAP502
|
2.9
|
32.9
|
1.0
|
|
CX
|
H:KCX201
|
2.9
|
27.4
|
1.0
|
|
C3
|
H:CAP502
|
3.0
|
32.1
|
1.0
|
|
CD
|
H:GLU204
|
3.1
|
31.8
|
1.0
|
|
CG
|
H:ASP203
|
3.1
|
30.9
|
1.0
|
|
OQ1
|
H:KCX201
|
3.3
|
30.0
|
1.0
|
|
OE2
|
H:GLU204
|
3.6
|
33.1
|
1.0
|
|
N
|
H:GLU204
|
3.7
|
27.2
|
1.0
|
|
NZ
|
H:LYS177
|
3.8
|
30.4
|
1.0
|
|
OD2
|
H:ASP203
|
3.8
|
34.7
|
1.0
|
|
CG2
|
H:THR173
|
3.9
|
27.9
|
1.0
|
|
ND2
|
V:ASN123
|
4.0
|
31.4
|
1.0
|
|
NE2
|
H:HIS294
|
4.0
|
25.0
|
1.0
|
|
NZ
|
H:LYS175
|
4.0
|
28.6
|
1.0
|
|
CA
|
H:ASP203
|
4.1
|
26.8
|
1.0
|
|
NZ
|
H:KCX201
|
4.1
|
25.7
|
1.0
|
|
CB
|
H:ASP203
|
4.1
|
26.6
|
1.0
|
|
O6
|
H:CAP502
|
4.2
|
33.5
|
1.0
|
|
C4
|
H:CAP502
|
4.3
|
34.0
|
1.0
|
|
C1
|
H:CAP502
|
4.3
|
32.4
|
1.0
|
|
OG1
|
H:THR173
|
4.3
|
33.9
|
1.0
|
|
CG
|
H:GLU204
|
4.4
|
25.9
|
1.0
|
|
C
|
H:ASP203
|
4.4
|
27.7
|
1.0
|
|
CB
|
H:GLU204
|
4.5
|
27.4
|
1.0
|
|
CD2
|
H:HIS294
|
4.6
|
21.6
|
1.0
|
|
CB
|
H:THR173
|
4.7
|
31.8
|
1.0
|
|
CA
|
H:GLU204
|
4.7
|
27.4
|
1.0
|
|
C5
|
H:CAP502
|
4.8
|
31.0
|
1.0
|
|
O1
|
H:CAP502
|
4.8
|
31.2
|
1.0
|
|
CE1
|
H:HIS294
|
5.0
|
25.0
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 1uwa
Go back to
Magnesium Binding Sites List in 1uwa
Magnesium binding site 5 out
of 8 in the L290F Mutant Rubisco From Chlamydomonas
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of L290F Mutant Rubisco From Chlamydomonas within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
K:Mg501
b:27.6
occ:1.00
|
OD1
|
K:ASP203
|
1.9
|
30.8
|
1.0
|
|
OQ2
|
K:KCX201
|
2.0
|
24.5
|
1.0
|
|
OE1
|
K:GLU204
|
2.1
|
30.4
|
1.0
|
|
O7
|
K:CAP502
|
2.2
|
32.3
|
1.0
|
|
O2
|
K:CAP502
|
2.2
|
32.8
|
1.0
|
|
O3
|
K:CAP502
|
2.2
|
32.1
|
1.0
|
|
C2
|
K:CAP502
|
2.8
|
33.0
|
1.0
|
|
C
|
K:CAP502
|
2.9
|
32.7
|
1.0
|
|
C3
|
K:CAP502
|
3.0
|
31.7
|
1.0
|
|
CG
|
K:ASP203
|
3.1
|
30.7
|
1.0
|
|
CX
|
K:KCX201
|
3.1
|
27.3
|
1.0
|
|
CD
|
K:GLU204
|
3.2
|
31.8
|
1.0
|
|
OQ1
|
K:KCX201
|
3.5
|
29.6
|
1.0
|
|
OE2
|
K:GLU204
|
3.6
|
33.0
|
1.0
|
|
NZ
|
K:LYS177
|
3.7
|
30.1
|
1.0
|
|
OD2
|
K:ASP203
|
3.7
|
34.6
|
1.0
|
|
N
|
K:GLU204
|
3.8
|
27.0
|
1.0
|
|
NZ
|
K:LYS175
|
3.9
|
28.2
|
1.0
|
|
CG2
|
K:THR173
|
3.9
|
27.9
|
1.0
|
|
ND2
|
R:ASN123
|
4.0
|
31.3
|
1.0
|
|
CA
|
K:ASP203
|
4.1
|
26.5
|
1.0
|
|
NE2
|
K:HIS294
|
4.1
|
25.0
|
1.0
|
|
CB
|
K:ASP203
|
4.1
|
26.7
|
1.0
|
|
O6
|
K:CAP502
|
4.2
|
33.1
|
1.0
|
|
NZ
|
K:KCX201
|
4.2
|
25.4
|
1.0
|
|
OG1
|
K:THR173
|
4.3
|
34.0
|
1.0
|
|
C1
|
K:CAP502
|
4.3
|
32.1
|
1.0
|
|
C4
|
K:CAP502
|
4.3
|
34.2
|
1.0
|
|
CG
|
K:GLU204
|
4.5
|
25.6
|
1.0
|
|
C
|
K:ASP203
|
4.5
|
27.4
|
1.0
|
|
CB
|
K:GLU204
|
4.6
|
27.5
|
1.0
|
|
CB
|
K:THR173
|
4.7
|
31.8
|
1.0
|
|
CD2
|
K:HIS294
|
4.7
|
21.6
|
1.0
|
|
O1
|
K:CAP502
|
4.8
|
30.9
|
1.0
|
|
CA
|
K:GLU204
|
4.8
|
27.1
|
1.0
|
|
C5
|
K:CAP502
|
4.9
|
30.8
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 1uwa
Go back to
Magnesium Binding Sites List in 1uwa
Magnesium binding site 6 out
of 8 in the L290F Mutant Rubisco From Chlamydomonas
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of L290F Mutant Rubisco From Chlamydomonas within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Mg501
b:27.5
occ:1.00
|
O3
|
O:CAP502
|
2.0
|
32.2
|
1.0
|
|
OQ2
|
O:KCX201
|
2.0
|
24.4
|
1.0
|
|
OD1
|
O:ASP203
|
2.0
|
31.0
|
1.0
|
|
OE1
|
O:GLU204
|
2.1
|
30.4
|
1.0
|
|
O7
|
O:CAP502
|
2.1
|
32.2
|
1.0
|
|
O2
|
O:CAP502
|
2.2
|
33.1
|
1.0
|
|
C2
|
O:CAP502
|
2.8
|
32.8
|
1.0
|
|
C
|
O:CAP502
|
2.9
|
32.9
|
1.0
|
|
C3
|
O:CAP502
|
2.9
|
32.0
|
1.0
|
|
CX
|
O:KCX201
|
3.0
|
27.5
|
1.0
|
|
CD
|
O:GLU204
|
3.2
|
31.5
|
1.0
|
|
CG
|
O:ASP203
|
3.3
|
30.7
|
1.0
|
|
OQ1
|
O:KCX201
|
3.3
|
29.6
|
1.0
|
|
OE2
|
O:GLU204
|
3.7
|
32.5
|
1.0
|
|
NZ
|
O:LYS177
|
3.8
|
30.0
|
1.0
|
|
N
|
O:GLU204
|
3.8
|
27.1
|
1.0
|
|
ND2
|
A:ASN123
|
3.9
|
31.2
|
1.0
|
|
OD2
|
O:ASP203
|
3.9
|
34.1
|
1.0
|
|
NE2
|
O:HIS294
|
3.9
|
25.3
|
1.0
|
|
NZ
|
O:LYS175
|
4.0
|
28.2
|
1.0
|
|
CG2
|
O:THR173
|
4.0
|
27.9
|
1.0
|
|
C4
|
O:CAP502
|
4.1
|
34.0
|
1.0
|
|
O6
|
O:CAP502
|
4.2
|
33.3
|
1.0
|
|
CA
|
O:ASP203
|
4.2
|
26.6
|
1.0
|
|
NZ
|
O:KCX201
|
4.2
|
25.6
|
1.0
|
|
C1
|
O:CAP502
|
4.3
|
32.1
|
1.0
|
|
CB
|
O:ASP203
|
4.3
|
26.3
|
1.0
|
|
OG1
|
O:THR173
|
4.3
|
34.4
|
1.0
|
|
CG
|
O:GLU204
|
4.4
|
25.7
|
1.0
|
|
C
|
O:ASP203
|
4.5
|
27.6
|
1.0
|
|
CD2
|
O:HIS294
|
4.6
|
21.6
|
1.0
|
|
CB
|
O:GLU204
|
4.6
|
27.6
|
1.0
|
|
C5
|
O:CAP502
|
4.7
|
30.5
|
1.0
|
|
CB
|
O:THR173
|
4.7
|
31.8
|
1.0
|
|
O1
|
O:CAP502
|
4.8
|
30.9
|
1.0
|
|
CA
|
O:GLU204
|
4.8
|
27.3
|
1.0
|
|
CE1
|
O:HIS294
|
4.9
|
25.2
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 1uwa
Go back to
Magnesium Binding Sites List in 1uwa
Magnesium binding site 7 out
of 8 in the L290F Mutant Rubisco From Chlamydomonas
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of L290F Mutant Rubisco From Chlamydomonas within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Mg501
b:28.1
occ:1.00
|
OD1
|
R:ASP203
|
1.9
|
31.2
|
1.0
|
|
OQ2
|
R:KCX201
|
2.0
|
24.1
|
1.0
|
|
O7
|
R:CAP502
|
2.1
|
32.6
|
1.0
|
|
OE1
|
R:GLU204
|
2.1
|
30.6
|
1.0
|
|
O2
|
R:CAP502
|
2.1
|
32.7
|
1.0
|
|
O3
|
R:CAP502
|
2.2
|
31.9
|
1.0
|
|
C2
|
R:CAP502
|
2.8
|
32.8
|
1.0
|
|
C
|
R:CAP502
|
2.9
|
32.7
|
1.0
|
|
C3
|
R:CAP502
|
3.0
|
32.0
|
1.0
|
|
CX
|
R:KCX201
|
3.1
|
27.4
|
1.0
|
|
CG
|
R:ASP203
|
3.1
|
30.9
|
1.0
|
|
CD
|
R:GLU204
|
3.2
|
31.8
|
1.0
|
|
OQ1
|
R:KCX201
|
3.4
|
29.8
|
1.0
|
|
OE2
|
R:GLU204
|
3.6
|
33.2
|
1.0
|
|
NZ
|
R:LYS177
|
3.7
|
30.3
|
1.0
|
|
OD2
|
R:ASP203
|
3.8
|
34.6
|
1.0
|
|
N
|
R:GLU204
|
3.8
|
27.0
|
1.0
|
|
NZ
|
R:LYS175
|
3.9
|
28.2
|
1.0
|
|
ND2
|
K:ASN123
|
3.9
|
31.1
|
1.0
|
|
CG2
|
R:THR173
|
4.0
|
27.9
|
1.0
|
|
NE2
|
R:HIS294
|
4.1
|
25.4
|
1.0
|
|
O6
|
R:CAP502
|
4.1
|
33.1
|
1.0
|
|
CA
|
R:ASP203
|
4.1
|
26.6
|
1.0
|
|
CB
|
R:ASP203
|
4.2
|
26.6
|
1.0
|
|
NZ
|
R:KCX201
|
4.2
|
25.8
|
1.0
|
|
C4
|
R:CAP502
|
4.3
|
33.9
|
1.0
|
|
C1
|
R:CAP502
|
4.3
|
32.3
|
1.0
|
|
OG1
|
R:THR173
|
4.3
|
34.3
|
1.0
|
|
CG
|
R:GLU204
|
4.4
|
25.8
|
1.0
|
|
C
|
R:ASP203
|
4.5
|
27.6
|
1.0
|
|
CB
|
R:GLU204
|
4.6
|
27.5
|
1.0
|
|
CB
|
R:THR173
|
4.7
|
31.7
|
1.0
|
|
CD2
|
R:HIS294
|
4.7
|
21.9
|
1.0
|
|
O1
|
R:CAP502
|
4.7
|
31.1
|
1.0
|
|
C5
|
R:CAP502
|
4.8
|
30.8
|
1.0
|
|
CA
|
R:GLU204
|
4.9
|
27.1
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 1uwa
Go back to
Magnesium Binding Sites List in 1uwa
Magnesium binding site 8 out
of 8 in the L290F Mutant Rubisco From Chlamydomonas
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of L290F Mutant Rubisco From Chlamydomonas within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
V:Mg501
b:27.4
occ:1.00
|
OD1
|
V:ASP203
|
1.9
|
30.9
|
1.0
|
|
OQ2
|
V:KCX201
|
2.1
|
24.0
|
1.0
|
|
OE1
|
V:GLU204
|
2.1
|
30.7
|
1.0
|
|
O3
|
V:CAP502
|
2.1
|
32.1
|
1.0
|
|
O7
|
V:CAP502
|
2.1
|
32.5
|
1.0
|
|
O2
|
V:CAP502
|
2.2
|
33.1
|
1.0
|
|
C2
|
V:CAP502
|
2.9
|
32.7
|
1.0
|
|
C
|
V:CAP502
|
2.9
|
32.9
|
1.0
|
|
C3
|
V:CAP502
|
3.0
|
32.0
|
1.0
|
|
CX
|
V:KCX201
|
3.1
|
27.3
|
1.0
|
|
CG
|
V:ASP203
|
3.1
|
30.8
|
1.0
|
|
CD
|
V:GLU204
|
3.1
|
31.8
|
1.0
|
|
OQ1
|
V:KCX201
|
3.4
|
29.6
|
1.0
|
|
OE2
|
V:GLU204
|
3.6
|
33.2
|
1.0
|
|
NZ
|
V:LYS177
|
3.7
|
30.3
|
1.0
|
|
OD2
|
V:ASP203
|
3.8
|
34.4
|
1.0
|
|
N
|
V:GLU204
|
3.8
|
27.3
|
1.0
|
|
NZ
|
V:LYS175
|
3.9
|
28.3
|
1.0
|
|
ND2
|
H:ASN123
|
3.9
|
31.1
|
1.0
|
|
CG2
|
V:THR173
|
4.0
|
27.8
|
1.0
|
|
NE2
|
V:HIS294
|
4.0
|
25.4
|
1.0
|
|
CA
|
V:ASP203
|
4.1
|
26.8
|
1.0
|
|
O6
|
V:CAP502
|
4.2
|
33.1
|
1.0
|
|
CB
|
V:ASP203
|
4.2
|
26.7
|
1.0
|
|
NZ
|
V:KCX201
|
4.2
|
25.8
|
1.0
|
|
C4
|
V:CAP502
|
4.2
|
34.0
|
1.0
|
|
C1
|
V:CAP502
|
4.3
|
32.4
|
1.0
|
|
OG1
|
V:THR173
|
4.4
|
34.1
|
1.0
|
|
CG
|
V:GLU204
|
4.4
|
25.6
|
1.0
|
|
C
|
V:ASP203
|
4.5
|
27.8
|
1.0
|
|
CB
|
V:GLU204
|
4.6
|
27.6
|
1.0
|
|
CD2
|
V:HIS294
|
4.6
|
22.1
|
1.0
|
|
CB
|
V:THR173
|
4.7
|
31.7
|
1.0
|
|
C5
|
V:CAP502
|
4.8
|
30.7
|
1.0
|
|
CA
|
V:GLU204
|
4.8
|
27.0
|
1.0
|
|
O1
|
V:CAP502
|
4.8
|
30.8
|
1.0
|
|
CE1
|
V:HIS294
|
5.0
|
25.0
|
1.0
|
|
Reference:
S.Karkehabadi,
T.C.Taylor,
R.J.Spreitzer,
I.Andersson.
Altered Intersubunit Interactions in Crystal Structures of Catalytically Compromised Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Biochemistry V. 44 113 2005.
ISSN: ISSN 0006-2960
PubMed: 15628851
DOI: 10.1021/BI047928E
Page generated: Tue Aug 13 14:56:17 2024
|
