Magnesium in PDB 5mz2: Rubisco From Thalassiosira Antarctica
Protein crystallography data
The structure of Rubisco From Thalassiosira Antarctica, PDB code: 5mz2
was solved by
I.Andersson,
K.Valegard,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
62.09 /
1.90
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
118.300,
220.100,
124.351,
90.00,
118.39,
90.00
|
R / Rfree (%)
|
14.3 /
17.6
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Rubisco From Thalassiosira Antarctica
(pdb code 5mz2). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 10 binding sites of Magnesium where determined in the
Rubisco From Thalassiosira Antarctica, PDB code: 5mz2:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Magnesium binding site 1 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 1 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg901
b:10.2
occ:1.00
|
OE2
|
A:GLU208
|
2.0
|
8.6
|
1.0
|
O6
|
A:CAP902
|
2.1
|
10.6
|
1.0
|
OQ1
|
A:KCX205
|
2.1
|
8.9
|
1.0
|
OD2
|
A:ASP207
|
2.1
|
15.3
|
1.0
|
O3
|
A:CAP902
|
2.2
|
9.2
|
1.0
|
O2
|
A:CAP902
|
2.3
|
9.7
|
1.0
|
C
|
A:CAP902
|
2.8
|
9.9
|
1.0
|
C2
|
A:CAP902
|
2.8
|
12.0
|
1.0
|
C3
|
A:CAP902
|
3.1
|
8.8
|
1.0
|
CD
|
A:GLU208
|
3.1
|
12.4
|
1.0
|
CX
|
A:KCX205
|
3.1
|
11.6
|
1.0
|
CG
|
A:ASP207
|
3.1
|
12.9
|
1.0
|
OQ2
|
A:KCX205
|
3.4
|
11.6
|
1.0
|
OE1
|
A:GLU208
|
3.5
|
14.3
|
1.0
|
NZ
|
A:LYS181
|
3.6
|
12.4
|
1.0
|
OD1
|
A:ASP207
|
3.7
|
15.0
|
1.0
|
ND2
|
B:ASN127
|
3.8
|
11.7
|
1.0
|
N
|
A:GLU208
|
3.8
|
8.7
|
1.0
|
NZ
|
A:LYS179
|
4.0
|
10.3
|
1.0
|
O7
|
A:CAP902
|
4.0
|
10.8
|
1.0
|
NE2
|
A:HIS297
|
4.1
|
8.3
|
1.0
|
CG2
|
A:THR177
|
4.1
|
8.2
|
1.0
|
CA
|
A:ASP207
|
4.2
|
8.0
|
1.0
|
CB
|
A:ASP207
|
4.2
|
8.1
|
1.0
|
C4
|
A:CAP902
|
4.3
|
12.1
|
1.0
|
NZ
|
A:KCX205
|
4.3
|
10.8
|
1.0
|
C1
|
A:CAP902
|
4.3
|
8.5
|
1.0
|
CG
|
A:GLU208
|
4.4
|
9.0
|
1.0
|
OG1
|
A:THR177
|
4.4
|
11.4
|
1.0
|
CD2
|
A:HIS297
|
4.5
|
7.2
|
1.0
|
C
|
A:ASP207
|
4.6
|
9.7
|
1.0
|
CB
|
A:GLU208
|
4.6
|
7.4
|
1.0
|
CB
|
A:THR177
|
4.8
|
8.4
|
1.0
|
C5
|
A:CAP902
|
4.8
|
10.9
|
1.0
|
CA
|
A:GLU208
|
4.8
|
9.7
|
1.0
|
O1
|
A:CAP902
|
4.8
|
9.6
|
1.0
|
CG
|
B:ASN127
|
4.9
|
12.1
|
1.0
|
|
Magnesium binding site 2 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 2 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg901
b:10.0
occ:1.00
|
OD2
|
C:ASP207
|
2.0
|
10.6
|
1.0
|
OQ2
|
C:KCX205
|
2.0
|
7.4
|
1.0
|
OE2
|
C:GLU208
|
2.1
|
8.8
|
1.0
|
O7
|
C:CAP902
|
2.1
|
8.8
|
1.0
|
O3
|
C:CAP902
|
2.2
|
8.4
|
1.0
|
O2
|
C:CAP902
|
2.2
|
7.3
|
1.0
|
C2
|
C:CAP902
|
2.8
|
9.1
|
1.0
|
C
|
C:CAP902
|
2.8
|
8.1
|
1.0
|
CX
|
C:KCX205
|
3.0
|
9.6
|
1.0
|
C3
|
C:CAP902
|
3.0
|
6.7
|
1.0
|
CD
|
C:GLU208
|
3.1
|
10.9
|
1.0
|
CG
|
C:ASP207
|
3.2
|
9.9
|
1.0
|
OQ1
|
C:KCX205
|
3.3
|
8.6
|
1.0
|
OE1
|
C:GLU208
|
3.5
|
12.3
|
1.0
|
NZ
|
C:LYS181
|
3.6
|
9.7
|
1.0
|
ND2
|
D:ASN127
|
3.8
|
8.3
|
1.0
|
OD1
|
C:ASP207
|
3.8
|
14.4
|
1.0
|
N
|
C:GLU208
|
3.9
|
5.2
|
1.0
|
NZ
|
C:LYS179
|
3.9
|
7.9
|
1.0
|
NE2
|
C:HIS297
|
4.0
|
8.3
|
1.0
|
CG2
|
C:THR177
|
4.0
|
7.1
|
1.0
|
O6
|
C:CAP902
|
4.1
|
9.5
|
1.0
|
CA
|
C:ASP207
|
4.2
|
6.9
|
1.0
|
NZ
|
C:KCX205
|
4.2
|
7.0
|
1.0
|
CB
|
C:ASP207
|
4.2
|
8.5
|
1.0
|
C4
|
C:CAP902
|
4.2
|
8.4
|
1.0
|
C1
|
C:CAP902
|
4.3
|
7.9
|
1.0
|
OG1
|
C:THR177
|
4.3
|
11.7
|
1.0
|
CG
|
C:GLU208
|
4.4
|
8.9
|
1.0
|
CD2
|
C:HIS297
|
4.5
|
6.8
|
1.0
|
C
|
C:ASP207
|
4.6
|
7.6
|
1.0
|
CB
|
C:GLU208
|
4.6
|
7.1
|
1.0
|
CB
|
C:THR177
|
4.7
|
10.3
|
1.0
|
C5
|
C:CAP902
|
4.8
|
8.5
|
1.0
|
O1
|
C:CAP902
|
4.8
|
10.2
|
1.0
|
CA
|
C:GLU208
|
4.9
|
5.9
|
1.0
|
CG
|
D:ASN127
|
4.9
|
8.7
|
1.0
|
|
Magnesium binding site 3 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 3 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg901
b:9.9
occ:1.00
|
OQ2
|
H:KCX205
|
2.0
|
5.5
|
1.0
|
OD2
|
H:ASP207
|
2.0
|
11.7
|
1.0
|
OE2
|
H:GLU208
|
2.0
|
8.9
|
1.0
|
O7
|
H:CAP902
|
2.1
|
9.2
|
1.0
|
O3
|
H:CAP902
|
2.1
|
8.1
|
1.0
|
O2
|
H:CAP902
|
2.3
|
6.9
|
1.0
|
C2
|
H:CAP902
|
2.8
|
10.0
|
1.0
|
C
|
H:CAP902
|
2.8
|
9.3
|
1.0
|
CX
|
H:KCX205
|
3.0
|
8.4
|
1.0
|
C3
|
H:CAP902
|
3.0
|
7.4
|
1.0
|
CD
|
H:GLU208
|
3.1
|
11.1
|
1.0
|
CG
|
H:ASP207
|
3.2
|
10.4
|
1.0
|
OQ1
|
H:KCX205
|
3.2
|
8.9
|
1.0
|
OE1
|
H:GLU208
|
3.5
|
13.2
|
1.0
|
NZ
|
H:LYS181
|
3.7
|
9.4
|
1.0
|
ND2
|
G:ASN127
|
3.8
|
8.7
|
1.0
|
N
|
H:GLU208
|
3.8
|
5.9
|
1.0
|
OD1
|
H:ASP207
|
3.9
|
13.8
|
1.0
|
NZ
|
H:LYS179
|
3.9
|
9.1
|
1.0
|
NE2
|
H:HIS297
|
4.0
|
8.3
|
1.0
|
O6
|
H:CAP902
|
4.1
|
8.9
|
1.0
|
CG2
|
H:THR177
|
4.1
|
7.5
|
1.0
|
NZ
|
H:KCX205
|
4.2
|
7.4
|
1.0
|
CA
|
H:ASP207
|
4.2
|
7.5
|
1.0
|
C4
|
H:CAP902
|
4.2
|
9.3
|
1.0
|
CB
|
H:ASP207
|
4.2
|
7.7
|
1.0
|
C1
|
H:CAP902
|
4.3
|
8.9
|
1.0
|
OG1
|
H:THR177
|
4.3
|
11.9
|
1.0
|
CG
|
H:GLU208
|
4.4
|
7.1
|
1.0
|
CD2
|
H:HIS297
|
4.4
|
7.1
|
1.0
|
CB
|
H:GLU208
|
4.5
|
7.4
|
1.0
|
C
|
H:ASP207
|
4.6
|
8.8
|
1.0
|
CB
|
H:THR177
|
4.7
|
10.1
|
1.0
|
C5
|
H:CAP902
|
4.8
|
8.4
|
1.0
|
O1
|
H:CAP902
|
4.8
|
10.7
|
1.0
|
CA
|
H:GLU208
|
4.8
|
5.6
|
1.0
|
CG
|
G:ASN127
|
4.9
|
9.9
|
1.0
|
CE1
|
H:HIS297
|
5.0
|
9.3
|
1.0
|
|
Magnesium binding site 4 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 4 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Mg901
b:8.5
occ:1.00
|
OD2
|
F:ASP207
|
2.0
|
9.2
|
1.0
|
OE2
|
F:GLU208
|
2.0
|
9.2
|
1.0
|
OQ2
|
F:KCX205
|
2.1
|
7.3
|
1.0
|
O7
|
F:CAP902
|
2.2
|
8.1
|
1.0
|
O3
|
F:CAP902
|
2.2
|
8.1
|
1.0
|
O2
|
F:CAP902
|
2.3
|
8.0
|
1.0
|
C2
|
F:CAP902
|
2.8
|
8.7
|
1.0
|
C
|
F:CAP902
|
2.9
|
9.8
|
1.0
|
C3
|
F:CAP902
|
3.0
|
6.4
|
1.0
|
CX
|
F:KCX205
|
3.1
|
9.9
|
1.0
|
CD
|
F:GLU208
|
3.1
|
8.1
|
1.0
|
CG
|
F:ASP207
|
3.2
|
11.3
|
1.0
|
OQ1
|
F:KCX205
|
3.3
|
9.5
|
1.0
|
OE1
|
F:GLU208
|
3.5
|
11.9
|
1.0
|
NZ
|
F:LYS181
|
3.6
|
9.2
|
1.0
|
ND2
|
E:ASN127
|
3.7
|
9.9
|
1.0
|
N
|
F:GLU208
|
3.8
|
6.3
|
1.0
|
OD1
|
F:ASP207
|
3.9
|
10.7
|
1.0
|
NZ
|
F:LYS179
|
4.0
|
7.9
|
1.0
|
NE2
|
F:HIS297
|
4.0
|
9.3
|
1.0
|
CG2
|
F:THR177
|
4.1
|
8.1
|
1.0
|
O6
|
F:CAP902
|
4.1
|
9.1
|
1.0
|
CA
|
F:ASP207
|
4.2
|
7.7
|
1.0
|
CB
|
F:ASP207
|
4.2
|
7.7
|
1.0
|
C4
|
F:CAP902
|
4.2
|
9.3
|
1.0
|
NZ
|
F:KCX205
|
4.2
|
7.7
|
1.0
|
C1
|
F:CAP902
|
4.3
|
7.9
|
1.0
|
CG
|
F:GLU208
|
4.4
|
6.7
|
1.0
|
OG1
|
F:THR177
|
4.4
|
10.2
|
1.0
|
CD2
|
F:HIS297
|
4.5
|
7.5
|
1.0
|
CB
|
F:GLU208
|
4.6
|
6.5
|
1.0
|
C
|
F:ASP207
|
4.6
|
8.1
|
1.0
|
CB
|
F:THR177
|
4.8
|
10.3
|
1.0
|
C5
|
F:CAP902
|
4.8
|
7.3
|
1.0
|
CG
|
E:ASN127
|
4.8
|
8.6
|
1.0
|
CA
|
F:GLU208
|
4.8
|
6.9
|
1.0
|
O1
|
F:CAP902
|
4.8
|
9.4
|
1.0
|
O
|
E:HOH1033
|
5.0
|
11.6
|
1.0
|
|
Magnesium binding site 5 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 5 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg901
b:9.4
occ:1.00
|
OD2
|
D:ASP207
|
2.0
|
8.6
|
1.0
|
OQ1
|
D:KCX205
|
2.0
|
6.9
|
1.0
|
OE2
|
D:GLU208
|
2.0
|
10.4
|
1.0
|
O6
|
D:CAP902
|
2.1
|
9.1
|
1.0
|
O3
|
D:CAP902
|
2.2
|
9.2
|
1.0
|
O2
|
D:CAP902
|
2.3
|
7.7
|
1.0
|
C
|
D:CAP902
|
2.9
|
9.4
|
1.0
|
C2
|
D:CAP902
|
2.9
|
8.9
|
1.0
|
CX
|
D:KCX205
|
3.0
|
8.7
|
1.0
|
C3
|
D:CAP902
|
3.0
|
8.7
|
1.0
|
CD
|
D:GLU208
|
3.1
|
10.8
|
1.0
|
CG
|
D:ASP207
|
3.2
|
10.4
|
1.0
|
OQ2
|
D:KCX205
|
3.3
|
9.2
|
1.0
|
OE1
|
D:GLU208
|
3.6
|
13.6
|
1.0
|
NZ
|
D:LYS181
|
3.7
|
10.4
|
1.0
|
ND2
|
C:ASN127
|
3.8
|
8.1
|
1.0
|
N
|
D:GLU208
|
3.8
|
6.2
|
1.0
|
OD1
|
D:ASP207
|
3.9
|
10.1
|
1.0
|
NZ
|
D:LYS179
|
3.9
|
7.1
|
1.0
|
CG2
|
D:THR177
|
4.0
|
7.0
|
1.0
|
NE2
|
D:HIS297
|
4.1
|
6.2
|
1.0
|
O7
|
D:CAP902
|
4.1
|
10.7
|
1.0
|
NZ
|
D:KCX205
|
4.2
|
7.3
|
1.0
|
CA
|
D:ASP207
|
4.2
|
7.5
|
1.0
|
CB
|
D:ASP207
|
4.2
|
7.3
|
1.0
|
C4
|
D:CAP902
|
4.3
|
9.7
|
1.0
|
OG1
|
D:THR177
|
4.3
|
11.2
|
1.0
|
C1
|
D:CAP902
|
4.4
|
8.3
|
1.0
|
CG
|
D:GLU208
|
4.4
|
6.5
|
1.0
|
CD2
|
D:HIS297
|
4.5
|
7.5
|
1.0
|
C
|
D:ASP207
|
4.5
|
6.4
|
1.0
|
CB
|
D:GLU208
|
4.5
|
6.8
|
1.0
|
CB
|
D:THR177
|
4.7
|
8.4
|
1.0
|
CA
|
D:GLU208
|
4.8
|
6.2
|
1.0
|
O1
|
D:CAP902
|
4.8
|
8.4
|
1.0
|
C5
|
D:CAP902
|
4.9
|
9.8
|
1.0
|
CG
|
C:ASN127
|
4.9
|
10.6
|
1.0
|
O
|
C:HOH1104
|
5.0
|
13.0
|
1.0
|
|
Magnesium binding site 6 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 6 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg901
b:11.2
occ:1.00
|
OD2
|
B:ASP207
|
2.0
|
11.6
|
1.0
|
OE2
|
B:GLU208
|
2.0
|
8.2
|
1.0
|
OQ1
|
B:KCX205
|
2.1
|
8.0
|
1.0
|
O6
|
B:CAP902
|
2.1
|
10.0
|
1.0
|
O3
|
B:CAP902
|
2.2
|
8.7
|
1.0
|
O2
|
B:CAP902
|
2.3
|
10.2
|
1.0
|
C
|
B:CAP902
|
2.8
|
10.3
|
1.0
|
C2
|
B:CAP902
|
2.9
|
11.4
|
1.0
|
CD
|
B:GLU208
|
3.1
|
12.0
|
1.0
|
C3
|
B:CAP902
|
3.1
|
8.9
|
1.0
|
CX
|
B:KCX205
|
3.1
|
11.7
|
1.0
|
CG
|
B:ASP207
|
3.2
|
10.6
|
1.0
|
OQ2
|
B:KCX205
|
3.4
|
10.1
|
1.0
|
OE1
|
B:GLU208
|
3.5
|
13.6
|
1.0
|
NZ
|
B:LYS181
|
3.6
|
11.5
|
1.0
|
ND2
|
A:ASN127
|
3.7
|
11.0
|
1.0
|
N
|
B:GLU208
|
3.8
|
8.1
|
1.0
|
OD1
|
B:ASP207
|
3.8
|
13.2
|
1.0
|
NZ
|
B:LYS179
|
3.9
|
10.0
|
1.0
|
CG2
|
B:THR177
|
4.0
|
9.3
|
1.0
|
O7
|
B:CAP902
|
4.1
|
11.6
|
1.0
|
NE2
|
B:HIS297
|
4.1
|
8.1
|
1.0
|
CA
|
B:ASP207
|
4.2
|
8.5
|
1.0
|
CB
|
B:ASP207
|
4.2
|
9.0
|
1.0
|
NZ
|
B:KCX205
|
4.3
|
9.0
|
1.0
|
C4
|
B:CAP902
|
4.3
|
10.9
|
1.0
|
C1
|
B:CAP902
|
4.3
|
9.6
|
1.0
|
CG
|
B:GLU208
|
4.4
|
9.6
|
1.0
|
OG1
|
B:THR177
|
4.4
|
12.1
|
1.0
|
CD2
|
B:HIS297
|
4.5
|
8.0
|
1.0
|
C
|
B:ASP207
|
4.5
|
8.8
|
1.0
|
CB
|
B:GLU208
|
4.6
|
7.4
|
1.0
|
CB
|
B:THR177
|
4.7
|
8.9
|
1.0
|
CA
|
B:GLU208
|
4.8
|
8.2
|
1.0
|
C5
|
B:CAP902
|
4.8
|
11.9
|
1.0
|
O1
|
B:CAP902
|
4.8
|
8.9
|
1.0
|
CG
|
A:ASN127
|
4.9
|
12.4
|
1.0
|
O
|
A:HOH1047
|
5.0
|
13.4
|
1.0
|
CE
|
B:LYS181
|
5.0
|
14.7
|
1.0
|
|
Magnesium binding site 7 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 7 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg901
b:8.9
occ:1.00
|
OD2
|
E:ASP207
|
2.0
|
9.7
|
1.0
|
OE2
|
E:GLU208
|
2.0
|
8.6
|
1.0
|
OQ2
|
E:KCX205
|
2.1
|
7.6
|
1.0
|
O7
|
E:CAP902
|
2.1
|
9.4
|
1.0
|
O3
|
E:CAP902
|
2.2
|
7.4
|
1.0
|
O2
|
E:CAP902
|
2.3
|
9.1
|
1.0
|
C
|
E:CAP902
|
2.8
|
10.1
|
1.0
|
C2
|
E:CAP902
|
2.8
|
9.5
|
1.0
|
C3
|
E:CAP902
|
3.0
|
7.0
|
1.0
|
CX
|
E:KCX205
|
3.1
|
10.2
|
1.0
|
CD
|
E:GLU208
|
3.1
|
10.4
|
1.0
|
CG
|
E:ASP207
|
3.2
|
11.7
|
1.0
|
OQ1
|
E:KCX205
|
3.3
|
10.0
|
1.0
|
OE1
|
E:GLU208
|
3.5
|
14.1
|
1.0
|
NZ
|
E:LYS181
|
3.6
|
9.5
|
1.0
|
ND2
|
F:ASN127
|
3.7
|
9.1
|
1.0
|
N
|
E:GLU208
|
3.9
|
6.1
|
1.0
|
OD1
|
E:ASP207
|
3.9
|
11.8
|
1.0
|
NZ
|
E:LYS179
|
3.9
|
8.6
|
1.0
|
NE2
|
E:HIS297
|
4.0
|
9.3
|
1.0
|
O6
|
E:CAP902
|
4.1
|
10.4
|
1.0
|
CG2
|
E:THR177
|
4.1
|
7.2
|
1.0
|
CA
|
E:ASP207
|
4.2
|
7.6
|
1.0
|
C4
|
E:CAP902
|
4.2
|
9.9
|
1.0
|
CB
|
E:ASP207
|
4.2
|
7.5
|
1.0
|
NZ
|
E:KCX205
|
4.2
|
6.7
|
1.0
|
C1
|
E:CAP902
|
4.3
|
7.9
|
1.0
|
CG
|
E:GLU208
|
4.4
|
8.8
|
1.0
|
OG1
|
E:THR177
|
4.4
|
11.8
|
1.0
|
CD2
|
E:HIS297
|
4.5
|
7.8
|
1.0
|
CB
|
E:GLU208
|
4.6
|
6.8
|
1.0
|
C
|
E:ASP207
|
4.6
|
8.1
|
1.0
|
CB
|
E:THR177
|
4.8
|
10.4
|
1.0
|
C5
|
E:CAP902
|
4.8
|
7.6
|
1.0
|
CG
|
F:ASN127
|
4.8
|
8.6
|
1.0
|
O1
|
E:CAP902
|
4.8
|
8.6
|
1.0
|
CA
|
E:GLU208
|
4.9
|
7.0
|
1.0
|
O
|
F:HOH1089
|
5.0
|
11.3
|
1.0
|
|
Magnesium binding site 8 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 8 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Mg901
b:9.4
occ:1.00
|
OQ1
|
G:KCX205
|
2.0
|
7.2
|
1.0
|
OD2
|
G:ASP207
|
2.0
|
8.7
|
1.0
|
OE2
|
G:GLU208
|
2.1
|
9.5
|
1.0
|
O6
|
G:CAP902
|
2.1
|
10.0
|
1.0
|
O3
|
G:CAP902
|
2.2
|
8.8
|
1.0
|
O2
|
G:CAP902
|
2.3
|
7.2
|
1.0
|
C
|
G:CAP902
|
2.9
|
8.8
|
1.0
|
C2
|
G:CAP902
|
2.9
|
8.0
|
1.0
|
CX
|
G:KCX205
|
3.0
|
9.7
|
1.0
|
C3
|
G:CAP902
|
3.0
|
9.2
|
1.0
|
CD
|
G:GLU208
|
3.1
|
9.7
|
1.0
|
CG
|
G:ASP207
|
3.2
|
11.8
|
1.0
|
OQ2
|
G:KCX205
|
3.4
|
9.3
|
1.0
|
OE1
|
G:GLU208
|
3.5
|
12.0
|
1.0
|
NZ
|
G:LYS181
|
3.7
|
9.2
|
1.0
|
ND2
|
H:ASN127
|
3.7
|
8.2
|
1.0
|
N
|
G:GLU208
|
3.8
|
6.2
|
1.0
|
OD1
|
G:ASP207
|
3.9
|
10.9
|
1.0
|
NZ
|
G:LYS179
|
3.9
|
8.3
|
1.0
|
NE2
|
G:HIS297
|
4.0
|
6.7
|
1.0
|
CG2
|
G:THR177
|
4.1
|
6.7
|
1.0
|
O7
|
G:CAP902
|
4.1
|
9.1
|
1.0
|
NZ
|
G:KCX205
|
4.2
|
6.5
|
1.0
|
CA
|
G:ASP207
|
4.2
|
8.0
|
1.0
|
CB
|
G:ASP207
|
4.2
|
7.7
|
1.0
|
C4
|
G:CAP902
|
4.3
|
8.9
|
1.0
|
OG1
|
G:THR177
|
4.3
|
9.8
|
1.0
|
C1
|
G:CAP902
|
4.3
|
7.3
|
1.0
|
CG
|
G:GLU208
|
4.4
|
6.8
|
1.0
|
CD2
|
G:HIS297
|
4.5
|
7.8
|
1.0
|
CB
|
G:GLU208
|
4.5
|
6.4
|
1.0
|
C
|
G:ASP207
|
4.6
|
6.7
|
1.0
|
CB
|
G:THR177
|
4.7
|
8.1
|
1.0
|
CA
|
G:GLU208
|
4.8
|
6.0
|
1.0
|
O1
|
G:CAP902
|
4.8
|
8.9
|
1.0
|
C5
|
G:CAP902
|
4.8
|
7.8
|
1.0
|
CG
|
H:ASN127
|
4.9
|
9.6
|
1.0
|
O
|
H:HOH1096
|
5.0
|
12.6
|
1.0
|
|
Magnesium binding site 9 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 9 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 9 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Mg201
b:10.9
occ:1.00
|
O
|
J:HOH428
|
2.2
|
22.8
|
1.0
|
O
|
K:HOH370
|
2.2
|
19.1
|
1.0
|
O
|
I:HOH308
|
2.2
|
24.9
|
1.0
|
O
|
I:HOH345
|
2.2
|
15.4
|
1.0
|
O
|
L:HOH406
|
2.2
|
15.1
|
1.0
|
O
|
J:HOH396
|
2.2
|
16.1
|
1.0
|
O
|
J:HOH346
|
4.2
|
12.6
|
1.0
|
O
|
I:HOH315
|
4.2
|
13.0
|
1.0
|
O
|
L:HOH349
|
4.2
|
14.0
|
1.0
|
O
|
K:HOH327
|
4.3
|
15.5
|
1.0
|
NZ
|
I:LYS126
|
4.3
|
17.8
|
1.0
|
O2
|
I:EDO203
|
4.4
|
40.9
|
1.0
|
NZ
|
K:LYS126
|
4.4
|
16.2
|
1.0
|
NZ
|
J:LYS126
|
4.5
|
16.8
|
1.0
|
NZ
|
L:LYS126
|
4.7
|
18.9
|
1.0
|
OD1
|
K:ASP112
|
4.9
|
20.3
|
1.0
|
OD1
|
I:ASP112
|
4.9
|
20.7
|
1.0
|
O2
|
J:EDO202
|
5.0
|
35.8
|
1.0
|
OD1
|
J:ASP112
|
5.0
|
19.1
|
1.0
|
CE
|
L:LYS126
|
5.0
|
16.2
|
1.0
|
|
Magnesium binding site 10 out
of 10 in 5mz2
Go back to
Magnesium Binding Sites List in 5mz2
Magnesium binding site 10 out
of 10 in the Rubisco From Thalassiosira Antarctica
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 10 of Rubisco From Thalassiosira Antarctica within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
M:Mg201
b:10.7
occ:1.00
|
O
|
O:HOH405
|
2.2
|
21.1
|
1.0
|
O
|
N:HOH391
|
2.2
|
18.8
|
1.0
|
O
|
O:HOH399
|
2.2
|
24.6
|
1.0
|
O
|
P:HOH335
|
2.2
|
14.8
|
1.0
|
O
|
M:HOH415
|
2.2
|
17.0
|
1.0
|
O
|
O:HOH360
|
2.2
|
15.7
|
1.0
|
O
|
O:HOH316
|
4.2
|
12.8
|
1.0
|
O
|
M:HOH341
|
4.2
|
12.8
|
1.0
|
O
|
N:HOH330
|
4.3
|
13.0
|
1.0
|
O
|
P:HOH311
|
4.3
|
12.9
|
1.0
|
NZ
|
P:LYS126
|
4.3
|
17.4
|
1.0
|
NZ
|
O:LYS126
|
4.4
|
16.8
|
1.0
|
NZ
|
N:LYS126
|
4.4
|
16.1
|
1.0
|
NZ
|
M:LYS126
|
4.7
|
20.1
|
1.0
|
OD1
|
P:ASP112
|
4.9
|
23.0
|
1.0
|
OD1
|
N:ASP112
|
4.9
|
19.4
|
1.0
|
OD1
|
M:ASP112
|
5.0
|
18.9
|
1.0
|
CE
|
M:LYS126
|
5.0
|
19.9
|
1.0
|
|
Reference:
K.Valegard,
P.J.Andralojc,
R.P.Haslam,
F.G.Pearce,
G.K.Eriksen,
P.J.Madgwick,
A.K.Kristoffersen,
M.Van Lun,
U.Klein,
H.C.Eilertsen,
M.A.J.Parry,
I.Andersson.
Structural and Functional Analyses of Rubisco From Arctic Diatom Species Reveal Unusual Posttranslational Modifications. J. Biol. Chem. V. 293 13033 2018.
ISSN: ESSN 1083-351X
PubMed: 29925588
DOI: 10.1074/JBC.RA118.003518
Page generated: Sun Sep 29 23:02:37 2024
|