Magnesium in PDB 2v63: Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
Enzymatic activity of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
All present enzymatic activity of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation:
4.1.1.39;
Protein crystallography data
The structure of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation, PDB code: 2v63
was solved by
S.Karkehabadi,
S.Satagopan,
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 /
1.80
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
121.377,
177.446,
122.568,
90.00,
117.65,
90.00
|
R / Rfree (%)
|
19.1 /
21.4
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
(pdb code 2v63). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation, PDB code: 2v63:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 2v63
Go back to
Magnesium Binding Sites List in 2v63
Magnesium binding site 1 out
of 8 in the Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg477
b:9.4
occ:1.00
|
OD1
|
A:ASP203
|
2.0
|
12.0
|
1.0
|
OQ1
|
A:KCX201
|
2.0
|
9.5
|
1.0
|
OE1
|
A:GLU204
|
2.0
|
10.8
|
1.0
|
O7
|
A:CAP476
|
2.1
|
13.4
|
1.0
|
O3
|
A:CAP476
|
2.1
|
11.9
|
1.0
|
O2
|
A:CAP476
|
2.3
|
12.0
|
1.0
|
C
|
A:CAP476
|
2.8
|
13.2
|
1.0
|
C2
|
A:CAP476
|
2.8
|
13.0
|
1.0
|
C3
|
A:CAP476
|
3.0
|
13.5
|
1.0
|
CX
|
A:KCX201
|
3.1
|
10.7
|
1.0
|
CD
|
A:GLU204
|
3.1
|
13.4
|
1.0
|
CG
|
A:ASP203
|
3.2
|
12.7
|
1.0
|
OQ2
|
A:KCX201
|
3.4
|
11.2
|
1.0
|
OE2
|
A:GLU204
|
3.6
|
15.3
|
1.0
|
NZ
|
A:LYS177
|
3.6
|
14.9
|
1.0
|
ND2
|
B:ASN123
|
3.8
|
14.5
|
1.0
|
N
|
A:GLU204
|
3.9
|
8.9
|
1.0
|
OD2
|
A:ASP203
|
3.9
|
16.2
|
1.0
|
NZ
|
A:LYS175
|
3.9
|
12.5
|
1.0
|
NE2
|
A:HIS294
|
4.0
|
7.8
|
1.0
|
O6
|
A:CAP476
|
4.0
|
13.6
|
1.0
|
CG2
|
A:THR173
|
4.1
|
12.7
|
1.0
|
CA
|
A:ASP203
|
4.2
|
9.4
|
1.0
|
CB
|
A:ASP203
|
4.2
|
10.0
|
1.0
|
C4
|
A:CAP476
|
4.2
|
14.8
|
1.0
|
NZ
|
A:KCX201
|
4.2
|
9.8
|
1.0
|
C1
|
A:CAP476
|
4.3
|
12.8
|
1.0
|
CG
|
A:GLU204
|
4.4
|
10.6
|
1.0
|
C
|
A:ASP203
|
4.6
|
9.0
|
1.0
|
CB
|
A:GLU204
|
4.6
|
9.7
|
1.0
|
OG1
|
A:THR173
|
4.6
|
14.7
|
1.0
|
CD2
|
A:HIS294
|
4.7
|
8.1
|
1.0
|
C5
|
A:CAP476
|
4.7
|
14.5
|
1.0
|
O1
|
A:CAP476
|
4.8
|
12.6
|
1.0
|
CE1
|
A:HIS294
|
4.8
|
8.3
|
1.0
|
CB
|
A:THR173
|
4.9
|
12.7
|
1.0
|
CA
|
A:GLU204
|
4.9
|
9.3
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 2v63
Go back to
Magnesium Binding Sites List in 2v63
Magnesium binding site 2 out
of 8 in the Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg476
b:9.1
occ:1.00
|
OQ1
|
B:KCX201
|
2.0
|
9.6
|
1.0
|
OE1
|
B:GLU204
|
2.0
|
10.4
|
1.0
|
OD1
|
B:ASP203
|
2.0
|
12.3
|
1.0
|
O3
|
B:CAP477
|
2.1
|
11.9
|
1.0
|
O7
|
B:CAP477
|
2.2
|
13.4
|
1.0
|
O2
|
B:CAP477
|
2.3
|
11.7
|
1.0
|
C2
|
B:CAP477
|
2.9
|
12.8
|
1.0
|
C
|
B:CAP477
|
2.9
|
13.1
|
1.0
|
CX
|
B:KCX201
|
3.0
|
10.6
|
1.0
|
C3
|
B:CAP477
|
3.0
|
13.2
|
1.0
|
CD
|
B:GLU204
|
3.1
|
13.2
|
1.0
|
CG
|
B:ASP203
|
3.2
|
12.7
|
1.0
|
OQ2
|
B:KCX201
|
3.3
|
11.4
|
1.0
|
OE2
|
B:GLU204
|
3.6
|
14.8
|
1.0
|
NZ
|
B:LYS177
|
3.7
|
14.9
|
1.0
|
ND2
|
A:ASN123
|
3.9
|
14.4
|
1.0
|
N
|
B:GLU204
|
3.9
|
8.8
|
1.0
|
NE2
|
B:HIS294
|
3.9
|
7.8
|
1.0
|
OD2
|
B:ASP203
|
4.0
|
16.1
|
1.0
|
NZ
|
B:LYS175
|
4.0
|
12.4
|
1.0
|
CG2
|
B:THR173
|
4.1
|
12.8
|
1.0
|
O6
|
B:CAP477
|
4.1
|
13.8
|
1.0
|
NZ
|
B:KCX201
|
4.2
|
9.8
|
1.0
|
CA
|
B:ASP203
|
4.2
|
9.2
|
1.0
|
C4
|
B:CAP477
|
4.2
|
14.6
|
1.0
|
CB
|
B:ASP203
|
4.2
|
10.0
|
1.0
|
C1
|
B:CAP477
|
4.3
|
12.5
|
1.0
|
CG
|
B:GLU204
|
4.4
|
10.4
|
1.0
|
CB
|
B:GLU204
|
4.5
|
9.4
|
1.0
|
OG1
|
B:THR173
|
4.6
|
14.6
|
1.0
|
C
|
B:ASP203
|
4.6
|
9.1
|
1.0
|
CD2
|
B:HIS294
|
4.6
|
8.3
|
1.0
|
C5
|
B:CAP477
|
4.7
|
14.4
|
1.0
|
CE1
|
B:HIS294
|
4.8
|
8.4
|
1.0
|
O1
|
B:CAP477
|
4.8
|
12.3
|
1.0
|
CB
|
B:THR173
|
4.8
|
12.5
|
1.0
|
CA
|
B:GLU204
|
4.8
|
9.2
|
1.0
|
O
|
A:HOH2092
|
4.9
|
19.6
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 2v63
Go back to
Magnesium Binding Sites List in 2v63
Magnesium binding site 3 out
of 8 in the Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg476
b:9.4
occ:1.00
|
OQ1
|
C:KCX201
|
1.9
|
9.3
|
1.0
|
OD1
|
C:ASP203
|
2.0
|
11.9
|
1.0
|
OE1
|
C:GLU204
|
2.0
|
11.1
|
1.0
|
O3
|
C:CAP477
|
2.1
|
11.4
|
1.0
|
O7
|
C:CAP477
|
2.2
|
13.4
|
1.0
|
O2
|
C:CAP477
|
2.3
|
11.7
|
1.0
|
C2
|
C:CAP477
|
2.9
|
12.8
|
1.0
|
C
|
C:CAP477
|
2.9
|
13.0
|
1.0
|
CX
|
C:KCX201
|
3.0
|
10.6
|
1.0
|
C3
|
C:CAP477
|
3.0
|
13.4
|
1.0
|
CD
|
C:GLU204
|
3.1
|
13.3
|
1.0
|
CG
|
C:ASP203
|
3.2
|
12.5
|
1.0
|
OQ2
|
C:KCX201
|
3.3
|
10.9
|
1.0
|
OE2
|
C:GLU204
|
3.5
|
15.2
|
1.0
|
NZ
|
C:LYS177
|
3.8
|
14.7
|
1.0
|
N
|
C:GLU204
|
3.8
|
8.8
|
1.0
|
ND2
|
D:ASN123
|
3.8
|
14.5
|
1.0
|
OD2
|
C:ASP203
|
3.9
|
16.3
|
1.0
|
NE2
|
C:HIS294
|
3.9
|
7.7
|
1.0
|
NZ
|
C:LYS175
|
4.0
|
12.2
|
1.0
|
CG2
|
C:THR173
|
4.1
|
12.8
|
1.0
|
O6
|
C:CAP477
|
4.1
|
13.4
|
1.0
|
CA
|
C:ASP203
|
4.1
|
9.3
|
1.0
|
NZ
|
C:KCX201
|
4.2
|
9.7
|
1.0
|
CB
|
C:ASP203
|
4.2
|
9.8
|
1.0
|
C4
|
C:CAP477
|
4.2
|
15.0
|
1.0
|
CG
|
C:GLU204
|
4.3
|
10.6
|
1.0
|
C1
|
C:CAP477
|
4.4
|
12.7
|
1.0
|
C
|
C:ASP203
|
4.5
|
8.8
|
1.0
|
CB
|
C:GLU204
|
4.6
|
9.5
|
1.0
|
CD2
|
C:HIS294
|
4.6
|
8.4
|
1.0
|
OG1
|
C:THR173
|
4.6
|
14.8
|
1.0
|
C5
|
C:CAP477
|
4.7
|
14.4
|
1.0
|
CA
|
C:GLU204
|
4.8
|
9.0
|
1.0
|
CE1
|
C:HIS294
|
4.8
|
8.0
|
1.0
|
O1
|
C:CAP477
|
4.8
|
12.8
|
1.0
|
CB
|
C:THR173
|
4.9
|
12.7
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 2v63
Go back to
Magnesium Binding Sites List in 2v63
Magnesium binding site 4 out
of 8 in the Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg476
b:9.5
occ:1.00
|
OD1
|
D:ASP203
|
2.0
|
11.3
|
1.0
|
OQ1
|
D:KCX201
|
2.0
|
10.3
|
1.0
|
OE1
|
D:GLU204
|
2.1
|
10.8
|
1.0
|
O3
|
D:CAP477
|
2.1
|
11.7
|
1.0
|
O7
|
D:CAP477
|
2.1
|
13.3
|
1.0
|
O2
|
D:CAP477
|
2.2
|
12.1
|
1.0
|
C
|
D:CAP477
|
2.9
|
13.2
|
1.0
|
C2
|
D:CAP477
|
2.9
|
13.1
|
1.0
|
CX
|
D:KCX201
|
3.0
|
10.3
|
1.0
|
C3
|
D:CAP477
|
3.0
|
13.6
|
1.0
|
CD
|
D:GLU204
|
3.1
|
13.6
|
1.0
|
CG
|
D:ASP203
|
3.2
|
12.5
|
1.0
|
OQ2
|
D:KCX201
|
3.3
|
11.6
|
1.0
|
OE2
|
D:GLU204
|
3.6
|
15.6
|
1.0
|
NZ
|
D:LYS177
|
3.6
|
14.4
|
1.0
|
ND2
|
C:ASN123
|
3.8
|
14.0
|
1.0
|
N
|
D:GLU204
|
3.9
|
9.3
|
1.0
|
NZ
|
D:LYS175
|
3.9
|
12.9
|
1.0
|
OD2
|
D:ASP203
|
4.0
|
15.8
|
1.0
|
NE2
|
D:HIS294
|
4.0
|
7.9
|
1.0
|
O6
|
D:CAP477
|
4.1
|
13.7
|
1.0
|
CG2
|
D:THR173
|
4.1
|
12.6
|
1.0
|
CA
|
D:ASP203
|
4.2
|
9.5
|
1.0
|
NZ
|
D:KCX201
|
4.2
|
10.1
|
1.0
|
CB
|
D:ASP203
|
4.2
|
9.9
|
1.0
|
C4
|
D:CAP477
|
4.2
|
14.5
|
1.0
|
C1
|
D:CAP477
|
4.3
|
12.8
|
1.0
|
CG
|
D:GLU204
|
4.4
|
10.7
|
1.0
|
C
|
D:ASP203
|
4.6
|
9.1
|
1.0
|
CB
|
D:GLU204
|
4.6
|
9.7
|
1.0
|
OG1
|
D:THR173
|
4.6
|
14.6
|
1.0
|
CD2
|
D:HIS294
|
4.7
|
7.7
|
1.0
|
C5
|
D:CAP477
|
4.7
|
14.6
|
1.0
|
O1
|
D:CAP477
|
4.8
|
12.6
|
1.0
|
CE1
|
D:HIS294
|
4.8
|
8.7
|
1.0
|
CB
|
D:THR173
|
4.8
|
12.6
|
1.0
|
CA
|
D:GLU204
|
4.9
|
9.4
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 2v63
Go back to
Magnesium Binding Sites List in 2v63
Magnesium binding site 5 out
of 8 in the Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg476
b:10.2
occ:1.00
|
OD1
|
E:ASP203
|
2.0
|
12.0
|
1.0
|
OQ1
|
E:KCX201
|
2.0
|
9.6
|
1.0
|
OE1
|
E:GLU204
|
2.1
|
11.0
|
1.0
|
O3
|
E:CAP477
|
2.1
|
11.7
|
1.0
|
O7
|
E:CAP477
|
2.1
|
13.1
|
1.0
|
O2
|
E:CAP477
|
2.2
|
12.1
|
1.0
|
C2
|
E:CAP477
|
2.8
|
13.0
|
1.0
|
C
|
E:CAP477
|
2.8
|
13.2
|
1.0
|
C3
|
E:CAP477
|
3.0
|
13.7
|
1.0
|
CX
|
E:KCX201
|
3.0
|
10.5
|
1.0
|
CD
|
E:GLU204
|
3.2
|
13.5
|
1.0
|
CG
|
E:ASP203
|
3.2
|
12.5
|
1.0
|
OQ2
|
E:KCX201
|
3.4
|
10.9
|
1.0
|
OE2
|
E:GLU204
|
3.6
|
15.5
|
1.0
|
NZ
|
E:LYS177
|
3.7
|
14.7
|
1.0
|
ND2
|
F:ASN123
|
3.8
|
14.2
|
1.0
|
NZ
|
E:LYS175
|
3.9
|
12.6
|
1.0
|
N
|
E:GLU204
|
3.9
|
9.2
|
1.0
|
OD2
|
E:ASP203
|
4.0
|
16.0
|
1.0
|
NE2
|
E:HIS294
|
4.0
|
8.3
|
1.0
|
O6
|
E:CAP477
|
4.1
|
13.7
|
1.0
|
CG2
|
E:THR173
|
4.1
|
13.0
|
1.0
|
CA
|
E:ASP203
|
4.2
|
9.4
|
1.0
|
C4
|
E:CAP477
|
4.2
|
14.9
|
1.0
|
CB
|
E:ASP203
|
4.2
|
10.1
|
1.0
|
NZ
|
E:KCX201
|
4.2
|
10.5
|
1.0
|
C1
|
E:CAP477
|
4.3
|
12.8
|
1.0
|
CG
|
E:GLU204
|
4.4
|
10.9
|
1.0
|
C
|
E:ASP203
|
4.6
|
9.1
|
1.0
|
OG1
|
E:THR173
|
4.6
|
14.7
|
1.0
|
CB
|
E:GLU204
|
4.6
|
9.7
|
1.0
|
CD2
|
E:HIS294
|
4.7
|
8.3
|
1.0
|
C5
|
E:CAP477
|
4.7
|
14.5
|
1.0
|
O1
|
E:CAP477
|
4.8
|
12.4
|
1.0
|
CB
|
E:THR173
|
4.8
|
12.6
|
1.0
|
CE1
|
E:HIS294
|
4.9
|
8.7
|
1.0
|
CA
|
E:GLU204
|
4.9
|
9.5
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 2v63
Go back to
Magnesium Binding Sites List in 2v63
Magnesium binding site 6 out
of 8 in the Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg476
b:10.9
occ:1.00
|
OD1
|
F:ASP203
|
2.0
|
12.2
|
1.0
|
OQ1
|
F:KCX201
|
2.0
|
9.1
|
1.0
|
OE1
|
F:GLU204
|
2.0
|
11.2
|
1.0
|
O7
|
F:CAP477
|
2.1
|
13.8
|
1.0
|
O3
|
F:CAP477
|
2.2
|
12.8
|
1.0
|
O2
|
F:CAP477
|
2.3
|
12.6
|
1.0
|
C
|
F:CAP477
|
2.9
|
13.6
|
1.0
|
C2
|
F:CAP477
|
2.9
|
13.4
|
1.0
|
CX
|
F:KCX201
|
3.0
|
10.8
|
1.0
|
C3
|
F:CAP477
|
3.1
|
13.7
|
1.0
|
CD
|
F:GLU204
|
3.1
|
13.1
|
1.0
|
CG
|
F:ASP203
|
3.2
|
12.9
|
1.0
|
OQ2
|
F:KCX201
|
3.3
|
11.3
|
1.0
|
OE2
|
F:GLU204
|
3.6
|
15.4
|
1.0
|
NZ
|
F:LYS177
|
3.7
|
14.9
|
1.0
|
ND2
|
E:ASN123
|
3.9
|
15.0
|
1.0
|
N
|
F:GLU204
|
3.9
|
9.5
|
1.0
|
OD2
|
F:ASP203
|
3.9
|
16.6
|
1.0
|
NZ
|
F:LYS175
|
3.9
|
12.8
|
1.0
|
NE2
|
F:HIS294
|
4.0
|
7.9
|
1.0
|
O6
|
F:CAP477
|
4.1
|
14.1
|
1.0
|
CG2
|
F:THR173
|
4.1
|
12.9
|
1.0
|
CA
|
F:ASP203
|
4.2
|
9.8
|
1.0
|
NZ
|
F:KCX201
|
4.2
|
9.8
|
1.0
|
CB
|
F:ASP203
|
4.2
|
10.0
|
1.0
|
C4
|
F:CAP477
|
4.3
|
15.1
|
1.0
|
C1
|
F:CAP477
|
4.3
|
13.0
|
1.0
|
CG
|
F:GLU204
|
4.4
|
10.9
|
1.0
|
C
|
F:ASP203
|
4.6
|
9.4
|
1.0
|
CB
|
F:GLU204
|
4.6
|
10.0
|
1.0
|
OG1
|
F:THR173
|
4.6
|
15.0
|
1.0
|
CD2
|
F:HIS294
|
4.7
|
8.2
|
1.0
|
C5
|
F:CAP477
|
4.8
|
14.9
|
1.0
|
O1
|
F:CAP477
|
4.8
|
13.3
|
1.0
|
CE1
|
F:HIS294
|
4.8
|
8.1
|
1.0
|
CA
|
F:GLU204
|
4.9
|
9.6
|
1.0
|
CB
|
F:THR173
|
4.9
|
13.0
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 2v63
Go back to
Magnesium Binding Sites List in 2v63
Magnesium binding site 7 out
of 8 in the Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg476
b:8.9
occ:1.00
|
OD1
|
G:ASP203
|
2.0
|
11.6
|
1.0
|
OE1
|
G:GLU204
|
2.0
|
10.7
|
1.0
|
OQ1
|
G:KCX201
|
2.0
|
9.7
|
1.0
|
O3
|
G:CAP477
|
2.2
|
12.0
|
1.0
|
O7
|
G:CAP477
|
2.2
|
13.7
|
1.0
|
O2
|
G:CAP477
|
2.2
|
12.3
|
1.0
|
C2
|
G:CAP477
|
2.9
|
13.1
|
1.0
|
C
|
G:CAP477
|
2.9
|
13.1
|
1.0
|
CX
|
G:KCX201
|
3.0
|
10.9
|
1.0
|
CD
|
G:GLU204
|
3.0
|
13.1
|
1.0
|
C3
|
G:CAP477
|
3.1
|
13.4
|
1.0
|
CG
|
G:ASP203
|
3.2
|
12.8
|
1.0
|
OQ2
|
G:KCX201
|
3.3
|
11.2
|
1.0
|
OE2
|
G:GLU204
|
3.5
|
14.9
|
1.0
|
NZ
|
G:LYS177
|
3.7
|
15.2
|
1.0
|
ND2
|
H:ASN123
|
3.8
|
14.4
|
1.0
|
N
|
G:GLU204
|
3.8
|
9.0
|
1.0
|
NE2
|
G:HIS294
|
3.9
|
7.8
|
1.0
|
OD2
|
G:ASP203
|
3.9
|
16.2
|
1.0
|
NZ
|
G:LYS175
|
4.0
|
12.6
|
1.0
|
O6
|
G:CAP477
|
4.1
|
13.2
|
1.0
|
CG2
|
G:THR173
|
4.1
|
12.6
|
1.0
|
NZ
|
G:KCX201
|
4.2
|
10.3
|
1.0
|
CA
|
G:ASP203
|
4.2
|
9.2
|
1.0
|
CB
|
G:ASP203
|
4.2
|
9.9
|
1.0
|
C4
|
G:CAP477
|
4.3
|
14.7
|
1.0
|
CG
|
G:GLU204
|
4.3
|
10.4
|
1.0
|
C1
|
G:CAP477
|
4.4
|
12.6
|
1.0
|
CB
|
G:GLU204
|
4.5
|
9.8
|
1.0
|
C
|
G:ASP203
|
4.5
|
8.8
|
1.0
|
OG1
|
G:THR173
|
4.7
|
14.7
|
1.0
|
CD2
|
G:HIS294
|
4.7
|
8.1
|
1.0
|
CE1
|
G:HIS294
|
4.8
|
8.5
|
1.0
|
C5
|
G:CAP477
|
4.8
|
14.4
|
1.0
|
CA
|
G:GLU204
|
4.8
|
9.3
|
1.0
|
O1
|
G:CAP477
|
4.8
|
12.1
|
1.0
|
CB
|
G:THR173
|
4.9
|
12.6
|
1.0
|
O
|
H:HOH2038
|
5.0
|
15.3
|
1.0
|
CG
|
H:ASN123
|
5.0
|
13.3
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 2v63
Go back to
Magnesium Binding Sites List in 2v63
Magnesium binding site 8 out
of 8 in the Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Crystal Structure of Rubisco From Chlamydomonas Reinhardtii with A Large-Subunit V331A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg476
b:9.2
occ:1.00
|
OQ1
|
H:KCX201
|
2.0
|
9.1
|
1.0
|
OD1
|
H:ASP203
|
2.0
|
12.3
|
1.0
|
OE1
|
H:GLU204
|
2.0
|
10.4
|
1.0
|
O7
|
H:CAP477
|
2.1
|
13.1
|
1.0
|
O3
|
H:CAP477
|
2.2
|
12.0
|
1.0
|
O2
|
H:CAP477
|
2.3
|
11.9
|
1.0
|
C
|
H:CAP477
|
2.8
|
13.2
|
1.0
|
C2
|
H:CAP477
|
2.8
|
12.8
|
1.0
|
CX
|
H:KCX201
|
3.0
|
10.8
|
1.0
|
C3
|
H:CAP477
|
3.0
|
13.5
|
1.0
|
CD
|
H:GLU204
|
3.1
|
13.8
|
1.0
|
CG
|
H:ASP203
|
3.2
|
12.4
|
1.0
|
OQ2
|
H:KCX201
|
3.3
|
11.2
|
1.0
|
OE2
|
H:GLU204
|
3.6
|
15.3
|
1.0
|
NZ
|
H:LYS177
|
3.7
|
14.9
|
1.0
|
ND2
|
G:ASN123
|
3.8
|
14.2
|
1.0
|
N
|
H:GLU204
|
3.9
|
8.7
|
1.0
|
NE2
|
H:HIS294
|
3.9
|
7.5
|
1.0
|
OD2
|
H:ASP203
|
4.0
|
16.3
|
1.0
|
NZ
|
H:LYS175
|
4.0
|
12.6
|
1.0
|
O6
|
H:CAP477
|
4.1
|
13.6
|
1.0
|
CG2
|
H:THR173
|
4.1
|
12.4
|
1.0
|
NZ
|
H:KCX201
|
4.2
|
9.4
|
1.0
|
C4
|
H:CAP477
|
4.2
|
14.6
|
1.0
|
CA
|
H:ASP203
|
4.2
|
9.3
|
1.0
|
CB
|
H:ASP203
|
4.2
|
10.1
|
1.0
|
C1
|
H:CAP477
|
4.3
|
13.1
|
1.0
|
CG
|
H:GLU204
|
4.4
|
10.5
|
1.0
|
C
|
H:ASP203
|
4.6
|
8.9
|
1.0
|
CB
|
H:GLU204
|
4.6
|
9.6
|
1.0
|
OG1
|
H:THR173
|
4.6
|
14.5
|
1.0
|
CD2
|
H:HIS294
|
4.6
|
8.1
|
1.0
|
C5
|
H:CAP477
|
4.7
|
14.5
|
1.0
|
CE1
|
H:HIS294
|
4.8
|
8.3
|
1.0
|
O1
|
H:CAP477
|
4.8
|
12.7
|
1.0
|
CA
|
H:GLU204
|
4.9
|
9.1
|
1.0
|
CB
|
H:THR173
|
4.9
|
12.7
|
1.0
|
CG
|
G:ASN123
|
5.0
|
13.3
|
1.0
|
|
Reference:
S.Karkehabadi,
S.Satagopan,
T.C.Taylor,
R.J.Spreitzer,
I.Andersson.
Structural Analysis of Altered Large-Subunit Loop- 6-Carboxy-Terminus Interactions That Influence Catalytic Efficiency and CO2 O2 Specificity of Ribulose-1,5-Bisphosphate Carboxylase Oxygenase Biochemistry V. 46 11080 2007.
ISSN: ISSN 0006-2960
PubMed: 17824672
DOI: 10.1021/BI701063F
Page generated: Wed Aug 14 04:59:47 2024
|