Magnesium in PDB 2v6a: Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
Enzymatic activity of Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
All present enzymatic activity of Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S:
4.1.1.39;
Protein crystallography data
The structure of Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S, PDB code: 2v6a
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 /
1.5
|
|
Space group
|
P 21 21 21
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
129.906,
196.629,
201.950,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
17.6 /
19.2
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
(pdb code 2v6a). 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 Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S, PDB code: 2v6a:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 2v6a
Go back to
Magnesium Binding Sites List in 2v6a
Magnesium binding site 1 out
of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
 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 Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg1476
b:13.0
occ:1.00
|
OD1
|
A:ASP203
|
2.0
|
14.3
|
1.0
|
|
OQ1
|
A:KCX201
|
2.0
|
12.7
|
1.0
|
|
OE1
|
A:GLU204
|
2.1
|
14.0
|
1.0
|
|
O7
|
A:CAP1477
|
2.1
|
14.4
|
1.0
|
|
O3
|
A:CAP1477
|
2.2
|
13.6
|
1.0
|
|
O2
|
A:CAP1477
|
2.3
|
14.3
|
1.0
|
|
C
|
A:CAP1477
|
2.8
|
15.2
|
1.0
|
|
C2
|
A:CAP1477
|
2.8
|
15.0
|
1.0
|
|
C3
|
A:CAP1477
|
3.0
|
15.0
|
1.0
|
|
CX
|
A:KCX201
|
3.0
|
14.2
|
1.0
|
|
CD
|
A:GLU204
|
3.1
|
14.7
|
1.0
|
|
CG
|
A:ASP203
|
3.2
|
15.8
|
1.0
|
|
OQ2
|
A:KCX201
|
3.3
|
14.7
|
1.0
|
|
OE2
|
A:GLU204
|
3.6
|
17.9
|
1.0
|
|
NZ
|
A:LYS177
|
3.7
|
15.6
|
1.0
|
|
ND2
|
B:ASN123
|
3.8
|
14.6
|
1.0
|
|
N
|
A:GLU204
|
3.9
|
12.3
|
1.0
|
|
NZ
|
A:LYS175
|
3.9
|
16.2
|
1.0
|
|
OD2
|
A:ASP203
|
3.9
|
18.9
|
1.0
|
|
NE2
|
A:HIS294
|
4.0
|
12.6
|
1.0
|
|
O6
|
A:CAP1477
|
4.0
|
16.6
|
1.0
|
|
CG2
|
A:THR173
|
4.0
|
15.9
|
1.0
|
|
C4
|
A:CAP1477
|
4.2
|
16.0
|
1.0
|
|
CA
|
A:ASP203
|
4.2
|
12.5
|
1.0
|
|
NZ
|
A:KCX201
|
4.2
|
12.5
|
1.0
|
|
CB
|
A:ASP203
|
4.2
|
12.9
|
1.0
|
|
C1
|
A:CAP1477
|
4.3
|
15.0
|
1.0
|
|
OG1
|
A:THR173
|
4.4
|
16.3
|
1.0
|
|
CG
|
A:GLU204
|
4.4
|
13.2
|
1.0
|
|
C
|
A:ASP203
|
4.6
|
12.5
|
1.0
|
|
CB
|
A:GLU204
|
4.6
|
12.9
|
1.0
|
|
CD2
|
A:HIS294
|
4.7
|
12.1
|
1.0
|
|
CB
|
A:THR173
|
4.7
|
14.6
|
1.0
|
|
C5
|
A:CAP1477
|
4.8
|
15.3
|
1.0
|
|
O1
|
A:CAP1477
|
4.8
|
14.1
|
1.0
|
|
CA
|
A:GLU204
|
4.9
|
12.3
|
1.0
|
|
CE1
|
A:HIS294
|
4.9
|
12.5
|
1.0
|
|
O
|
B:HOH1047
|
5.0
|
20.0
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 2v6a
Go back to
Magnesium Binding Sites List in 2v6a
Magnesium binding site 2 out
of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
 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 Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg1476
b:13.0
occ:1.00
|
OD1
|
B:ASP203
|
2.0
|
15.1
|
1.0
|
|
OE1
|
B:GLU204
|
2.0
|
13.6
|
1.0
|
|
OQ1
|
B:KCX201
|
2.0
|
12.4
|
1.0
|
|
O7
|
B:CAP1477
|
2.1
|
14.3
|
1.0
|
|
O3
|
B:CAP1477
|
2.2
|
14.0
|
1.0
|
|
O2
|
B:CAP1477
|
2.3
|
15.5
|
1.0
|
|
C
|
B:CAP1477
|
2.8
|
15.0
|
1.0
|
|
C2
|
B:CAP1477
|
2.8
|
14.7
|
1.0
|
|
CX
|
B:KCX201
|
3.0
|
12.9
|
1.0
|
|
C3
|
B:CAP1477
|
3.0
|
14.7
|
1.0
|
|
CD
|
B:GLU204
|
3.1
|
16.4
|
1.0
|
|
CG
|
B:ASP203
|
3.2
|
15.0
|
1.0
|
|
OQ2
|
B:KCX201
|
3.4
|
15.3
|
1.0
|
|
OE2
|
B:GLU204
|
3.6
|
19.4
|
1.0
|
|
NZ
|
B:LYS177
|
3.7
|
17.7
|
1.0
|
|
ND2
|
A:ASN123
|
3.8
|
15.9
|
1.0
|
|
N
|
B:GLU204
|
3.8
|
11.9
|
1.0
|
|
NZ
|
B:LYS175
|
3.9
|
15.8
|
1.0
|
|
OD2
|
B:ASP203
|
3.9
|
18.5
|
1.0
|
|
NE2
|
B:HIS294
|
4.0
|
13.3
|
1.0
|
|
O6
|
B:CAP1477
|
4.0
|
16.1
|
1.0
|
|
CG2
|
B:THR173
|
4.0
|
15.8
|
1.0
|
|
CA
|
B:ASP203
|
4.2
|
12.2
|
1.0
|
|
NZ
|
B:KCX201
|
4.2
|
12.6
|
1.0
|
|
C4
|
B:CAP1477
|
4.2
|
17.1
|
1.0
|
|
CB
|
B:ASP203
|
4.2
|
12.5
|
1.0
|
|
C1
|
B:CAP1477
|
4.3
|
14.2
|
1.0
|
|
OG1
|
B:THR173
|
4.4
|
16.5
|
1.0
|
|
CG
|
B:GLU204
|
4.4
|
13.2
|
1.0
|
|
C
|
B:ASP203
|
4.6
|
12.1
|
1.0
|
|
CB
|
B:GLU204
|
4.6
|
12.6
|
1.0
|
|
CD2
|
B:HIS294
|
4.6
|
12.3
|
1.0
|
|
CB
|
B:THR173
|
4.7
|
14.5
|
1.0
|
|
C5
|
B:CAP1477
|
4.8
|
16.1
|
1.0
|
|
O1
|
B:CAP1477
|
4.8
|
14.5
|
1.0
|
|
CA
|
B:GLU204
|
4.8
|
11.7
|
1.0
|
|
CE1
|
B:HIS294
|
4.8
|
12.2
|
1.0
|
|
CG
|
A:ASN123
|
5.0
|
14.8
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 2v6a
Go back to
Magnesium Binding Sites List in 2v6a
Magnesium binding site 3 out
of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
 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 Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg1476
b:13.9
occ:1.00
|
OD1
|
C:ASP203
|
2.0
|
15.7
|
1.0
|
|
OE1
|
C:GLU204
|
2.0
|
13.2
|
1.0
|
|
OQ1
|
C:KCX201
|
2.1
|
13.8
|
1.0
|
|
O7
|
C:CAP1477
|
2.1
|
16.4
|
1.0
|
|
O3
|
C:CAP1477
|
2.2
|
14.7
|
1.0
|
|
O2
|
C:CAP1477
|
2.2
|
15.8
|
1.0
|
|
C
|
C:CAP1477
|
2.8
|
16.2
|
1.0
|
|
C2
|
C:CAP1477
|
2.8
|
15.9
|
1.0
|
|
C3
|
C:CAP1477
|
3.0
|
16.4
|
1.0
|
|
CD
|
C:GLU204
|
3.1
|
13.6
|
1.0
|
|
CX
|
C:KCX201
|
3.1
|
13.1
|
1.0
|
|
CG
|
C:ASP203
|
3.2
|
16.6
|
1.0
|
|
OQ2
|
C:KCX201
|
3.4
|
15.4
|
1.0
|
|
OE2
|
C:GLU204
|
3.5
|
17.1
|
1.0
|
|
NZ
|
C:LYS177
|
3.6
|
17.2
|
1.0
|
|
ND2
|
D:ASN123
|
3.8
|
17.3
|
1.0
|
|
N
|
C:GLU204
|
3.9
|
12.3
|
1.0
|
|
OD2
|
C:ASP203
|
3.9
|
19.8
|
1.0
|
|
NZ
|
C:LYS175
|
3.9
|
15.9
|
1.0
|
|
NE2
|
C:HIS294
|
4.0
|
13.0
|
1.0
|
|
O6
|
C:CAP1477
|
4.0
|
16.9
|
1.0
|
|
CG2
|
C:THR173
|
4.1
|
15.9
|
1.0
|
|
CA
|
C:ASP203
|
4.2
|
13.0
|
1.0
|
|
C4
|
C:CAP1477
|
4.2
|
17.6
|
1.0
|
|
CB
|
C:ASP203
|
4.2
|
13.4
|
1.0
|
|
NZ
|
C:KCX201
|
4.3
|
13.1
|
1.0
|
|
C1
|
C:CAP1477
|
4.3
|
16.5
|
1.0
|
|
CG
|
C:GLU204
|
4.4
|
13.6
|
1.0
|
|
OG1
|
C:THR173
|
4.4
|
17.5
|
1.0
|
|
CB
|
C:GLU204
|
4.6
|
13.0
|
1.0
|
|
C
|
C:ASP203
|
4.6
|
12.9
|
1.0
|
|
CD2
|
C:HIS294
|
4.7
|
14.2
|
1.0
|
|
CB
|
C:THR173
|
4.7
|
15.8
|
1.0
|
|
O1
|
C:CAP1477
|
4.8
|
15.9
|
1.0
|
|
C5
|
C:CAP1477
|
4.8
|
16.7
|
1.0
|
|
CA
|
C:GLU204
|
4.9
|
12.8
|
1.0
|
|
CE1
|
C:HIS294
|
4.9
|
13.7
|
1.0
|
|
O
|
D:HOH1038
|
5.0
|
21.1
|
1.0
|
|
CG
|
D:ASN123
|
5.0
|
16.4
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 2v6a
Go back to
Magnesium Binding Sites List in 2v6a
Magnesium binding site 4 out
of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
 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 Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg1476
b:13.3
occ:1.00
|
OD1
|
D:ASP203
|
2.0
|
14.6
|
1.0
|
|
OE1
|
D:GLU204
|
2.0
|
13.9
|
1.0
|
|
OQ1
|
D:KCX201
|
2.0
|
12.3
|
1.0
|
|
O7
|
D:CAP1477
|
2.1
|
14.5
|
1.0
|
|
O3
|
D:CAP1477
|
2.2
|
14.2
|
1.0
|
|
O2
|
D:CAP1477
|
2.2
|
14.4
|
1.0
|
|
C2
|
D:CAP1477
|
2.8
|
15.6
|
1.0
|
|
C
|
D:CAP1477
|
2.8
|
15.4
|
1.0
|
|
C3
|
D:CAP1477
|
3.0
|
15.3
|
1.0
|
|
CX
|
D:KCX201
|
3.0
|
13.5
|
1.0
|
|
CD
|
D:GLU204
|
3.1
|
14.4
|
1.0
|
|
CG
|
D:ASP203
|
3.2
|
16.1
|
1.0
|
|
OQ2
|
D:KCX201
|
3.3
|
15.1
|
1.0
|
|
OE2
|
D:GLU204
|
3.6
|
17.8
|
1.0
|
|
NZ
|
D:LYS177
|
3.7
|
17.3
|
1.0
|
|
ND2
|
C:ASN123
|
3.8
|
16.8
|
1.0
|
|
N
|
D:GLU204
|
3.9
|
11.9
|
1.0
|
|
OD2
|
D:ASP203
|
3.9
|
18.4
|
1.0
|
|
NZ
|
D:LYS175
|
3.9
|
16.5
|
1.0
|
|
NE2
|
D:HIS294
|
4.0
|
13.3
|
1.0
|
|
O6
|
D:CAP1477
|
4.1
|
15.6
|
1.0
|
|
CG2
|
D:THR173
|
4.1
|
16.3
|
1.0
|
|
C4
|
D:CAP1477
|
4.2
|
16.0
|
1.0
|
|
NZ
|
D:KCX201
|
4.2
|
13.3
|
1.0
|
|
CA
|
D:ASP203
|
4.2
|
12.5
|
1.0
|
|
CB
|
D:ASP203
|
4.2
|
13.5
|
1.0
|
|
C1
|
D:CAP1477
|
4.3
|
15.9
|
1.0
|
|
CG
|
D:GLU204
|
4.4
|
13.0
|
1.0
|
|
OG1
|
D:THR173
|
4.4
|
17.0
|
1.0
|
|
CB
|
D:GLU204
|
4.6
|
12.5
|
1.0
|
|
C
|
D:ASP203
|
4.6
|
12.3
|
1.0
|
|
CD2
|
D:HIS294
|
4.7
|
13.4
|
1.0
|
|
CB
|
D:THR173
|
4.7
|
15.0
|
1.0
|
|
C5
|
D:CAP1477
|
4.7
|
14.3
|
1.0
|
|
O1
|
D:CAP1477
|
4.8
|
14.7
|
1.0
|
|
CA
|
D:GLU204
|
4.8
|
12.0
|
1.0
|
|
CE1
|
D:HIS294
|
4.9
|
11.9
|
1.0
|
|
CG
|
C:ASN123
|
5.0
|
15.6
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 2v6a
Go back to
Magnesium Binding Sites List in 2v6a
Magnesium binding site 5 out
of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
 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 Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg1476
b:13.7
occ:1.00
|
OD1
|
E:ASP203
|
2.0
|
15.3
|
1.0
|
|
OE1
|
E:GLU204
|
2.0
|
14.4
|
1.0
|
|
OQ1
|
E:KCX201
|
2.1
|
14.2
|
1.0
|
|
O7
|
E:CAP1477
|
2.1
|
14.6
|
1.0
|
|
O2
|
E:CAP1477
|
2.2
|
15.6
|
1.0
|
|
O3
|
E:CAP1477
|
2.2
|
15.3
|
1.0
|
|
C
|
E:CAP1477
|
2.8
|
15.1
|
1.0
|
|
C2
|
E:CAP1477
|
2.8
|
14.7
|
1.0
|
|
C3
|
E:CAP1477
|
3.1
|
14.9
|
1.0
|
|
CX
|
E:KCX201
|
3.1
|
14.5
|
1.0
|
|
CD
|
E:GLU204
|
3.1
|
15.2
|
1.0
|
|
CG
|
E:ASP203
|
3.2
|
15.9
|
1.0
|
|
OQ2
|
E:KCX201
|
3.4
|
15.2
|
1.0
|
|
OE2
|
E:GLU204
|
3.6
|
18.1
|
1.0
|
|
NZ
|
E:LYS177
|
3.7
|
17.7
|
1.0
|
|
N
|
E:GLU204
|
3.9
|
12.3
|
1.0
|
|
OD2
|
E:ASP203
|
3.9
|
19.2
|
1.0
|
|
ND2
|
F:ASN123
|
3.9
|
15.3
|
1.0
|
|
NZ
|
E:LYS175
|
3.9
|
16.0
|
1.0
|
|
NE2
|
E:HIS294
|
4.0
|
12.5
|
1.0
|
|
O6
|
E:CAP1477
|
4.0
|
15.9
|
1.0
|
|
CG2
|
E:THR173
|
4.1
|
16.4
|
1.0
|
|
C4
|
E:CAP1477
|
4.2
|
16.3
|
1.0
|
|
CA
|
E:ASP203
|
4.2
|
12.4
|
1.0
|
|
CB
|
E:ASP203
|
4.2
|
13.1
|
1.0
|
|
NZ
|
E:KCX201
|
4.3
|
13.1
|
1.0
|
|
C1
|
E:CAP1477
|
4.3
|
15.0
|
1.0
|
|
OG1
|
E:THR173
|
4.4
|
16.7
|
1.0
|
|
CG
|
E:GLU204
|
4.4
|
13.3
|
1.0
|
|
CB
|
E:GLU204
|
4.6
|
13.3
|
1.0
|
|
C
|
E:ASP203
|
4.6
|
12.2
|
1.0
|
|
CD2
|
E:HIS294
|
4.6
|
12.6
|
1.0
|
|
CB
|
E:THR173
|
4.7
|
14.8
|
1.0
|
|
O1
|
E:CAP1477
|
4.7
|
13.7
|
1.0
|
|
C5
|
E:CAP1477
|
4.8
|
16.0
|
1.0
|
|
CA
|
E:GLU204
|
4.8
|
12.2
|
1.0
|
|
CE1
|
E:HIS294
|
4.8
|
12.9
|
1.0
|
|
O
|
F:HOH1048
|
5.0
|
21.6
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 2v6a
Go back to
Magnesium Binding Sites List in 2v6a
Magnesium binding site 6 out
of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
 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 Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg1476
b:13.2
occ:1.00
|
OD1
|
F:ASP203
|
2.0
|
16.0
|
1.0
|
|
OQ1
|
F:KCX201
|
2.0
|
12.9
|
1.0
|
|
OE1
|
F:GLU204
|
2.1
|
13.3
|
1.0
|
|
O7
|
F:CAP1477
|
2.1
|
15.0
|
1.0
|
|
O3
|
F:CAP1477
|
2.1
|
16.1
|
1.0
|
|
O2
|
F:CAP1477
|
2.2
|
14.7
|
1.0
|
|
C2
|
F:CAP1477
|
2.8
|
15.0
|
1.0
|
|
C
|
F:CAP1477
|
2.8
|
15.1
|
1.0
|
|
C3
|
F:CAP1477
|
3.0
|
15.0
|
1.0
|
|
CX
|
F:KCX201
|
3.1
|
14.2
|
1.0
|
|
CD
|
F:GLU204
|
3.1
|
16.0
|
1.0
|
|
CG
|
F:ASP203
|
3.2
|
15.7
|
1.0
|
|
OQ2
|
F:KCX201
|
3.3
|
15.4
|
1.0
|
|
OE2
|
F:GLU204
|
3.6
|
17.2
|
1.0
|
|
NZ
|
F:LYS177
|
3.7
|
16.2
|
1.0
|
|
ND2
|
E:ASN123
|
3.8
|
15.3
|
1.0
|
|
N
|
F:GLU204
|
3.9
|
12.1
|
1.0
|
|
NZ
|
F:LYS175
|
3.9
|
17.3
|
1.0
|
|
OD2
|
F:ASP203
|
3.9
|
18.8
|
1.0
|
|
NE2
|
F:HIS294
|
3.9
|
14.0
|
1.0
|
|
O6
|
F:CAP1477
|
4.0
|
15.5
|
1.0
|
|
CG2
|
F:THR173
|
4.1
|
16.9
|
1.0
|
|
C4
|
F:CAP1477
|
4.2
|
17.1
|
1.0
|
|
CA
|
F:ASP203
|
4.2
|
12.3
|
1.0
|
|
NZ
|
F:KCX201
|
4.2
|
13.1
|
1.0
|
|
CB
|
F:ASP203
|
4.3
|
12.9
|
1.0
|
|
C1
|
F:CAP1477
|
4.3
|
14.4
|
1.0
|
|
OG1
|
F:THR173
|
4.4
|
16.6
|
1.0
|
|
CG
|
F:GLU204
|
4.4
|
12.8
|
1.0
|
|
C
|
F:ASP203
|
4.6
|
12.4
|
1.0
|
|
CB
|
F:GLU204
|
4.6
|
12.5
|
1.0
|
|
CD2
|
F:HIS294
|
4.6
|
13.8
|
1.0
|
|
CB
|
F:THR173
|
4.7
|
15.1
|
1.0
|
|
C5
|
F:CAP1477
|
4.8
|
17.1
|
1.0
|
|
O1
|
F:CAP1477
|
4.8
|
13.4
|
1.0
|
|
CE1
|
F:HIS294
|
4.8
|
12.3
|
1.0
|
|
CA
|
F:GLU204
|
4.9
|
12.2
|
1.0
|
|
O
|
E:HOH1048
|
5.0
|
21.5
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 2v6a
Go back to
Magnesium Binding Sites List in 2v6a
Magnesium binding site 7 out
of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
 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 Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg1476
b:12.2
occ:1.00
|
OD1
|
G:ASP203
|
2.0
|
15.6
|
1.0
|
|
OE1
|
G:GLU204
|
2.0
|
12.9
|
1.0
|
|
OQ1
|
G:KCX201
|
2.0
|
13.3
|
1.0
|
|
O7
|
G:CAP1477
|
2.1
|
13.5
|
1.0
|
|
O3
|
G:CAP1477
|
2.1
|
15.0
|
1.0
|
|
O2
|
G:CAP1477
|
2.2
|
14.2
|
1.0
|
|
C
|
G:CAP1477
|
2.8
|
14.5
|
1.0
|
|
C2
|
G:CAP1477
|
2.8
|
14.0
|
1.0
|
|
C3
|
G:CAP1477
|
3.0
|
14.3
|
1.0
|
|
CX
|
G:KCX201
|
3.1
|
13.1
|
1.0
|
|
CD
|
G:GLU204
|
3.1
|
14.2
|
1.0
|
|
CG
|
G:ASP203
|
3.2
|
16.0
|
1.0
|
|
OQ2
|
G:KCX201
|
3.4
|
13.6
|
1.0
|
|
OE2
|
G:GLU204
|
3.6
|
18.0
|
1.0
|
|
NZ
|
G:LYS177
|
3.7
|
17.3
|
1.0
|
|
ND2
|
H:ASN123
|
3.8
|
16.0
|
1.0
|
|
N
|
G:GLU204
|
3.9
|
12.1
|
1.0
|
|
OD2
|
G:ASP203
|
3.9
|
19.1
|
1.0
|
|
NE2
|
G:HIS294
|
3.9
|
12.0
|
1.0
|
|
NZ
|
G:LYS175
|
3.9
|
15.3
|
1.0
|
|
O6
|
G:CAP1477
|
4.0
|
15.9
|
1.0
|
|
CG2
|
G:THR173
|
4.1
|
15.4
|
1.0
|
|
C4
|
G:CAP1477
|
4.2
|
16.1
|
1.0
|
|
CA
|
G:ASP203
|
4.2
|
12.2
|
1.0
|
|
NZ
|
G:KCX201
|
4.2
|
12.6
|
1.0
|
|
CB
|
G:ASP203
|
4.2
|
12.8
|
1.0
|
|
C1
|
G:CAP1477
|
4.3
|
14.4
|
1.0
|
|
OG1
|
G:THR173
|
4.4
|
16.2
|
1.0
|
|
CG
|
G:GLU204
|
4.4
|
11.9
|
1.0
|
|
C
|
G:ASP203
|
4.6
|
12.2
|
1.0
|
|
CB
|
G:GLU204
|
4.6
|
13.1
|
1.0
|
|
CD2
|
G:HIS294
|
4.6
|
12.8
|
1.0
|
|
CB
|
G:THR173
|
4.7
|
14.3
|
1.0
|
|
C5
|
G:CAP1477
|
4.7
|
16.2
|
1.0
|
|
O1
|
G:CAP1477
|
4.8
|
14.2
|
1.0
|
|
CE1
|
G:HIS294
|
4.8
|
11.7
|
1.0
|
|
CA
|
G:GLU204
|
4.9
|
12.0
|
1.0
|
|
CG
|
H:ASN123
|
5.0
|
15.0
|
1.0
|
|
O
|
H:HOH1046
|
5.0
|
18.6
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 2v6a
Go back to
Magnesium Binding Sites List in 2v6a
Magnesium binding site 8 out
of 8 in the Crystal Structure of Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S
 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 Chlamydomonas Reinhardtii Rubisco with Large-Subunit Mutations V331A, G344S within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg1476
b:13.7
occ:1.00
|
OD1
|
H:ASP203
|
2.0
|
15.9
|
1.0
|
|
OQ1
|
H:KCX201
|
2.0
|
12.8
|
1.0
|
|
OE1
|
H:GLU204
|
2.0
|
14.8
|
1.0
|
|
O3
|
H:CAP1477
|
2.1
|
14.6
|
1.0
|
|
O7
|
H:CAP1477
|
2.1
|
14.7
|
1.0
|
|
O2
|
H:CAP1477
|
2.2
|
15.5
|
1.0
|
|
C2
|
H:CAP1477
|
2.8
|
15.2
|
1.0
|
|
C
|
H:CAP1477
|
2.8
|
15.3
|
1.0
|
|
CX
|
H:KCX201
|
3.0
|
12.8
|
1.0
|
|
C3
|
H:CAP1477
|
3.0
|
15.1
|
1.0
|
|
CD
|
H:GLU204
|
3.1
|
15.7
|
1.0
|
|
CG
|
H:ASP203
|
3.2
|
17.2
|
1.0
|
|
OQ2
|
H:KCX201
|
3.3
|
16.4
|
1.0
|
|
OE2
|
H:GLU204
|
3.6
|
17.9
|
1.0
|
|
NZ
|
H:LYS177
|
3.6
|
17.5
|
1.0
|
|
OD2
|
H:ASP203
|
3.9
|
19.5
|
1.0
|
|
ND2
|
G:ASN123
|
3.9
|
16.0
|
1.0
|
|
N
|
H:GLU204
|
3.9
|
12.6
|
1.0
|
|
NZ
|
H:LYS175
|
3.9
|
16.2
|
1.0
|
|
NE2
|
H:HIS294
|
3.9
|
12.7
|
1.0
|
|
O6
|
H:CAP1477
|
4.0
|
16.2
|
1.0
|
|
CG2
|
H:THR173
|
4.1
|
15.9
|
1.0
|
|
C4
|
H:CAP1477
|
4.2
|
16.7
|
1.0
|
|
NZ
|
H:KCX201
|
4.2
|
12.7
|
1.0
|
|
CA
|
H:ASP203
|
4.2
|
12.9
|
1.0
|
|
CB
|
H:ASP203
|
4.2
|
13.7
|
1.0
|
|
C1
|
H:CAP1477
|
4.3
|
16.0
|
1.0
|
|
OG1
|
H:THR173
|
4.3
|
16.8
|
1.0
|
|
CG
|
H:GLU204
|
4.4
|
13.8
|
1.0
|
|
C
|
H:ASP203
|
4.6
|
13.1
|
1.0
|
|
CB
|
H:GLU204
|
4.6
|
13.3
|
1.0
|
|
CD2
|
H:HIS294
|
4.6
|
13.2
|
1.0
|
|
CB
|
H:THR173
|
4.7
|
15.3
|
1.0
|
|
O1
|
H:CAP1477
|
4.7
|
14.9
|
1.0
|
|
C5
|
H:CAP1477
|
4.8
|
15.7
|
1.0
|
|
CA
|
H:GLU204
|
4.9
|
12.4
|
1.0
|
|
CE1
|
H:HIS294
|
4.9
|
14.1
|
1.0
|
|
O
|
G:HOH1043
|
5.0
|
21.2
|
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: Mon Dec 14 07:41:11 2020
|
