Magnesium in PDB 1uzh: A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
Enzymatic activity of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
All present enzymatic activity of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme:
4.1.1.39;
Protein crystallography data
The structure of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme, PDB code: 1uzh
was solved by
S.Karkehabadi,
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 /
2.20
|
|
Space group
|
P 21 21 2
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
220.820,
223.969,
111.752,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
16 /
19.3
|
Magnesium Binding Sites:
The binding sites of Magnesium atom in the A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
(pdb code 1uzh). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme, PDB code: 1uzh:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 1uzh
Go back to
Magnesium Binding Sites List in 1uzh
Magnesium binding site 1 out
of 8 in the A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg476
b:17.6
occ:1.00
|
OQ2
|
A:KCX201
|
2.0
|
15.0
|
1.0
|
|
OD1
|
A:ASP203
|
2.0
|
16.9
|
1.0
|
|
O3
|
A:CAP477
|
2.1
|
17.4
|
1.0
|
|
OE1
|
A:GLU204
|
2.1
|
16.8
|
1.0
|
|
O7
|
A:CAP477
|
2.3
|
16.5
|
1.0
|
|
O2
|
A:CAP477
|
2.3
|
23.9
|
1.0
|
|
CX
|
A:KCX201
|
2.9
|
15.9
|
1.0
|
|
C2
|
A:CAP477
|
2.9
|
17.2
|
1.0
|
|
C
|
A:CAP477
|
3.0
|
17.9
|
1.0
|
|
C3
|
A:CAP477
|
3.0
|
19.0
|
1.0
|
|
OQ1
|
A:KCX201
|
3.1
|
15.2
|
1.0
|
|
CD
|
A:GLU204
|
3.2
|
15.8
|
1.0
|
|
CG
|
A:ASP203
|
3.2
|
17.4
|
1.0
|
|
OE2
|
A:GLU204
|
3.6
|
18.0
|
1.0
|
|
N
|
A:GLU204
|
3.7
|
15.2
|
1.0
|
|
CG2
|
A:THR173
|
3.9
|
11.9
|
1.0
|
|
OD2
|
A:ASP203
|
3.9
|
20.4
|
1.0
|
|
NZ
|
A:LYS177
|
3.9
|
15.1
|
1.0
|
|
ND2
|
B:ASN123
|
4.0
|
18.2
|
1.0
|
|
NE2
|
A:HIS294
|
4.0
|
14.5
|
1.0
|
|
NZ
|
A:LYS175
|
4.0
|
14.4
|
1.0
|
|
CA
|
A:ASP203
|
4.1
|
14.9
|
1.0
|
|
NZ
|
A:KCX201
|
4.1
|
13.7
|
1.0
|
|
CB
|
A:ASP203
|
4.2
|
14.5
|
1.0
|
|
OG1
|
A:THR173
|
4.2
|
17.6
|
1.0
|
|
C4
|
A:CAP477
|
4.3
|
22.1
|
1.0
|
|
O6
|
A:CAP477
|
4.3
|
19.3
|
1.0
|
|
C1
|
A:CAP477
|
4.4
|
14.1
|
1.0
|
|
CG
|
A:GLU204
|
4.4
|
13.3
|
1.0
|
|
C
|
A:ASP203
|
4.4
|
15.8
|
1.0
|
|
CB
|
A:GLU204
|
4.5
|
15.0
|
1.0
|
|
CD2
|
A:HIS294
|
4.6
|
12.1
|
1.0
|
|
CB
|
A:THR173
|
4.6
|
17.2
|
1.0
|
|
C5
|
A:CAP477
|
4.7
|
15.0
|
1.0
|
|
CA
|
A:GLU204
|
4.7
|
14.9
|
1.0
|
|
O1
|
A:CAP477
|
4.8
|
20.5
|
1.0
|
|
CE1
|
A:HIS294
|
5.0
|
15.6
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 1uzh
Go back to
Magnesium Binding Sites List in 1uzh
Magnesium binding site 2 out
of 8 in the A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg476
b:13.0
occ:1.00
|
OQ2
|
B:KCX201
|
2.1
|
15.1
|
1.0
|
|
OD1
|
B:ASP203
|
2.1
|
17.3
|
1.0
|
|
OE1
|
B:GLU204
|
2.1
|
16.6
|
1.0
|
|
O7
|
B:CAP477
|
2.1
|
18.1
|
1.0
|
|
O3
|
B:CAP477
|
2.1
|
14.3
|
1.0
|
|
O2
|
B:CAP477
|
2.2
|
22.0
|
1.0
|
|
C2
|
B:CAP477
|
2.8
|
18.7
|
1.0
|
|
C
|
B:CAP477
|
2.9
|
19.4
|
1.0
|
|
C3
|
B:CAP477
|
3.0
|
15.2
|
1.0
|
|
CX
|
B:KCX201
|
3.1
|
16.1
|
1.0
|
|
CD
|
B:GLU204
|
3.1
|
16.1
|
1.0
|
|
CG
|
B:ASP203
|
3.2
|
17.4
|
1.0
|
|
OQ1
|
B:KCX201
|
3.3
|
15.1
|
1.0
|
|
OE2
|
B:GLU204
|
3.6
|
17.7
|
1.0
|
|
NZ
|
B:LYS177
|
3.7
|
14.8
|
1.0
|
|
ND2
|
A:ASN123
|
3.8
|
18.4
|
1.0
|
|
N
|
B:GLU204
|
3.8
|
15.2
|
1.0
|
|
OD2
|
B:ASP203
|
3.8
|
20.2
|
1.0
|
|
NZ
|
B:LYS175
|
3.9
|
14.3
|
1.0
|
|
CG2
|
B:THR173
|
3.9
|
12.0
|
1.0
|
|
NE2
|
B:HIS294
|
4.0
|
13.9
|
1.0
|
|
O6
|
B:CAP477
|
4.1
|
20.1
|
1.0
|
|
CA
|
B:ASP203
|
4.2
|
14.8
|
1.0
|
|
C4
|
B:CAP477
|
4.2
|
16.5
|
1.0
|
|
OG1
|
B:THR173
|
4.2
|
17.5
|
1.0
|
|
CB
|
B:ASP203
|
4.3
|
14.6
|
1.0
|
|
NZ
|
B:KCX201
|
4.3
|
13.1
|
1.0
|
|
C1
|
B:CAP477
|
4.3
|
18.1
|
1.0
|
|
CG
|
B:GLU204
|
4.4
|
13.4
|
1.0
|
|
C
|
B:ASP203
|
4.5
|
16.1
|
1.0
|
|
CB
|
B:GLU204
|
4.6
|
14.8
|
1.0
|
|
CD2
|
B:HIS294
|
4.6
|
12.2
|
1.0
|
|
CB
|
B:THR173
|
4.7
|
17.4
|
1.0
|
|
C5
|
B:CAP477
|
4.7
|
15.9
|
1.0
|
|
CA
|
B:GLU204
|
4.8
|
15.4
|
1.0
|
|
O1
|
B:CAP477
|
4.8
|
19.2
|
1.0
|
|
O
|
A:HOH2043
|
4.9
|
19.7
|
1.0
|
|
CE1
|
B:HIS294
|
4.9
|
15.3
|
1.0
|
|
CG
|
A:ASN123
|
5.0
|
19.5
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 1uzh
Go back to
Magnesium Binding Sites List in 1uzh
Magnesium binding site 3 out
of 8 in the A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Mg476
b:13.6
occ:1.00
|
OD1
|
E:ASP203
|
2.0
|
16.9
|
1.0
|
|
OE1
|
E:GLU204
|
2.0
|
17.0
|
1.0
|
|
OQ2
|
E:KCX201
|
2.0
|
15.0
|
1.0
|
|
O7
|
E:CAP477
|
2.0
|
20.2
|
1.0
|
|
O3
|
E:CAP477
|
2.2
|
24.2
|
1.0
|
|
O2
|
E:CAP477
|
2.4
|
19.9
|
1.0
|
|
C
|
E:CAP477
|
2.9
|
20.7
|
1.0
|
|
C2
|
E:CAP477
|
2.9
|
20.2
|
1.0
|
|
CD
|
E:GLU204
|
3.0
|
16.0
|
1.0
|
|
CX
|
E:KCX201
|
3.0
|
16.1
|
1.0
|
|
C3
|
E:CAP477
|
3.1
|
19.1
|
1.0
|
|
CG
|
E:ASP203
|
3.1
|
17.8
|
1.0
|
|
OQ1
|
E:KCX201
|
3.3
|
15.2
|
1.0
|
|
OE2
|
E:GLU204
|
3.4
|
18.0
|
1.0
|
|
N
|
E:GLU204
|
3.7
|
15.8
|
1.0
|
|
NZ
|
E:LYS177
|
3.7
|
15.4
|
1.0
|
|
OD2
|
E:ASP203
|
3.8
|
20.5
|
1.0
|
|
ND2
|
K:ASN123
|
3.9
|
18.4
|
1.0
|
|
CG2
|
E:THR173
|
3.9
|
11.8
|
1.0
|
|
NE2
|
E:HIS294
|
4.0
|
13.3
|
1.0
|
|
NZ
|
E:LYS175
|
4.0
|
14.5
|
1.0
|
|
CA
|
E:ASP203
|
4.1
|
15.0
|
1.0
|
|
CB
|
E:ASP203
|
4.1
|
14.1
|
1.0
|
|
O6
|
E:CAP477
|
4.2
|
23.7
|
1.0
|
|
NZ
|
E:KCX201
|
4.2
|
13.4
|
1.0
|
|
CG
|
E:GLU204
|
4.3
|
13.8
|
1.0
|
|
OG1
|
E:THR173
|
4.3
|
17.6
|
1.0
|
|
C4
|
E:CAP477
|
4.4
|
22.2
|
1.0
|
|
C
|
E:ASP203
|
4.4
|
15.9
|
1.0
|
|
C1
|
E:CAP477
|
4.4
|
19.1
|
1.0
|
|
CB
|
E:GLU204
|
4.5
|
15.1
|
1.0
|
|
CD2
|
E:HIS294
|
4.6
|
12.1
|
1.0
|
|
CB
|
E:THR173
|
4.7
|
17.3
|
1.0
|
|
CA
|
E:GLU204
|
4.7
|
15.1
|
1.0
|
|
C5
|
E:CAP477
|
4.8
|
19.0
|
1.0
|
|
O1
|
E:CAP477
|
4.8
|
21.1
|
1.0
|
|
CE1
|
E:HIS294
|
5.0
|
15.6
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 1uzh
Go back to
Magnesium Binding Sites List in 1uzh
Magnesium binding site 4 out
of 8 in the A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Mg476
b:16.5
occ:1.00
|
O7
|
H:CAP477
|
2.0
|
18.4
|
1.0
|
|
OD1
|
H:ASP203
|
2.0
|
17.3
|
1.0
|
|
OQ2
|
H:KCX201
|
2.1
|
15.0
|
1.0
|
|
OE1
|
H:GLU204
|
2.1
|
16.6
|
1.0
|
|
O3
|
H:CAP477
|
2.2
|
21.1
|
1.0
|
|
O2
|
H:CAP477
|
2.4
|
23.7
|
1.0
|
|
C
|
H:CAP477
|
2.8
|
20.0
|
1.0
|
|
C2
|
H:CAP477
|
2.9
|
22.0
|
1.0
|
|
CX
|
H:KCX201
|
3.1
|
15.8
|
1.0
|
|
C3
|
H:CAP477
|
3.1
|
18.9
|
1.0
|
|
CD
|
H:GLU204
|
3.1
|
15.9
|
1.0
|
|
CG
|
H:ASP203
|
3.2
|
17.6
|
1.0
|
|
OQ1
|
H:KCX201
|
3.3
|
15.4
|
1.0
|
|
OE2
|
H:GLU204
|
3.5
|
17.6
|
1.0
|
|
NZ
|
H:LYS177
|
3.7
|
15.4
|
1.0
|
|
OD2
|
H:ASP203
|
3.8
|
20.5
|
1.0
|
|
N
|
H:GLU204
|
3.8
|
15.5
|
1.0
|
|
ND2
|
R:ASN123
|
3.9
|
18.0
|
1.0
|
|
NZ
|
H:LYS175
|
3.9
|
14.6
|
1.0
|
|
CG2
|
H:THR173
|
4.0
|
12.1
|
1.0
|
|
NE2
|
H:HIS294
|
4.0
|
14.3
|
1.0
|
|
O6
|
H:CAP477
|
4.1
|
17.0
|
1.0
|
|
CA
|
H:ASP203
|
4.2
|
15.1
|
1.0
|
|
OG1
|
H:THR173
|
4.2
|
17.6
|
1.0
|
|
C4
|
H:CAP477
|
4.2
|
18.9
|
1.0
|
|
CB
|
H:ASP203
|
4.2
|
14.5
|
1.0
|
|
NZ
|
H:KCX201
|
4.3
|
13.5
|
1.0
|
|
C1
|
H:CAP477
|
4.4
|
23.3
|
1.0
|
|
CG
|
H:GLU204
|
4.4
|
13.6
|
1.0
|
|
C
|
H:ASP203
|
4.5
|
16.2
|
1.0
|
|
CB
|
H:GLU204
|
4.6
|
15.0
|
1.0
|
|
C5
|
H:CAP477
|
4.6
|
22.5
|
1.0
|
|
CB
|
H:THR173
|
4.6
|
17.2
|
1.0
|
|
CD2
|
H:HIS294
|
4.7
|
12.2
|
1.0
|
|
O1
|
H:CAP477
|
4.8
|
21.5
|
1.0
|
|
CA
|
H:GLU204
|
4.8
|
15.4
|
1.0
|
|
CE1
|
H:HIS294
|
5.0
|
15.6
|
1.0
|
|
O
|
R:HOH2042
|
5.0
|
21.6
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 1uzh
Go back to
Magnesium Binding Sites List in 1uzh
Magnesium binding site 5 out
of 8 in the A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
K:Mg476
b:19.3
occ:1.00
|
OD1
|
K:ASP203
|
2.0
|
16.9
|
1.0
|
|
OE1
|
K:GLU204
|
2.0
|
16.8
|
1.0
|
|
OQ2
|
K:KCX201
|
2.1
|
15.0
|
1.0
|
|
O7
|
K:CAP477
|
2.2
|
15.2
|
1.0
|
|
O3
|
K:CAP477
|
2.2
|
20.2
|
1.0
|
|
O2
|
K:CAP477
|
2.4
|
21.6
|
1.0
|
|
C
|
K:CAP477
|
3.0
|
18.1
|
1.0
|
|
C2
|
K:CAP477
|
3.0
|
16.2
|
1.0
|
|
CD
|
K:GLU204
|
3.0
|
15.7
|
1.0
|
|
C3
|
K:CAP477
|
3.1
|
17.2
|
1.0
|
|
CX
|
K:KCX201
|
3.1
|
15.8
|
1.0
|
|
CG
|
K:ASP203
|
3.2
|
17.5
|
1.0
|
|
OQ1
|
K:KCX201
|
3.3
|
15.5
|
1.0
|
|
OE2
|
K:GLU204
|
3.3
|
17.7
|
1.0
|
|
N
|
K:GLU204
|
3.7
|
15.6
|
1.0
|
|
NZ
|
K:LYS177
|
3.7
|
15.0
|
1.0
|
|
ND2
|
E:ASN123
|
3.8
|
17.9
|
1.0
|
|
OD2
|
K:ASP203
|
3.8
|
20.2
|
1.0
|
|
NE2
|
K:HIS294
|
4.0
|
14.1
|
1.0
|
|
CG2
|
K:THR173
|
4.0
|
11.7
|
1.0
|
|
NZ
|
K:LYS175
|
4.1
|
14.4
|
1.0
|
|
CA
|
K:ASP203
|
4.1
|
14.9
|
1.0
|
|
CB
|
K:ASP203
|
4.2
|
14.5
|
1.0
|
|
O6
|
K:CAP477
|
4.2
|
17.7
|
1.0
|
|
NZ
|
K:KCX201
|
4.3
|
13.7
|
1.0
|
|
C4
|
K:CAP477
|
4.3
|
20.8
|
1.0
|
|
CG
|
K:GLU204
|
4.3
|
13.7
|
1.0
|
|
C1
|
K:CAP477
|
4.4
|
20.1
|
1.0
|
|
C
|
K:ASP203
|
4.4
|
16.0
|
1.0
|
|
OG1
|
K:THR173
|
4.4
|
17.5
|
1.0
|
|
CB
|
K:GLU204
|
4.5
|
14.9
|
1.0
|
|
CD2
|
K:HIS294
|
4.6
|
12.2
|
1.0
|
|
CA
|
K:GLU204
|
4.7
|
15.0
|
1.0
|
|
C5
|
K:CAP477
|
4.7
|
13.7
|
1.0
|
|
CB
|
K:THR173
|
4.8
|
17.2
|
1.0
|
|
O1
|
K:CAP477
|
4.9
|
18.9
|
1.0
|
|
CE1
|
K:HIS294
|
4.9
|
15.5
|
1.0
|
|
CG
|
E:ASN123
|
4.9
|
19.6
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 1uzh
Go back to
Magnesium Binding Sites List in 1uzh
Magnesium binding site 6 out
of 8 in the A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Mg476
b:15.4
occ:1.00
|
OD1
|
O:ASP203
|
1.9
|
17.3
|
1.0
|
|
OE1
|
O:GLU204
|
2.0
|
16.8
|
1.0
|
|
OQ2
|
O:KCX201
|
2.1
|
14.9
|
1.0
|
|
O7
|
O:CAP477
|
2.2
|
12.2
|
1.0
|
|
O3
|
O:CAP477
|
2.2
|
19.4
|
1.0
|
|
O2
|
O:CAP477
|
2.3
|
23.3
|
1.0
|
|
C2
|
O:CAP477
|
3.0
|
18.9
|
1.0
|
|
C
|
O:CAP477
|
3.0
|
16.9
|
1.0
|
|
CX
|
O:KCX201
|
3.1
|
15.8
|
1.0
|
|
CD
|
O:GLU204
|
3.1
|
16.1
|
1.0
|
|
CG
|
O:ASP203
|
3.1
|
17.7
|
1.0
|
|
C3
|
O:CAP477
|
3.1
|
20.7
|
1.0
|
|
OQ1
|
O:KCX201
|
3.3
|
15.3
|
1.0
|
|
OE2
|
O:GLU204
|
3.5
|
17.8
|
1.0
|
|
NZ
|
O:LYS177
|
3.7
|
14.8
|
1.0
|
|
OD2
|
O:ASP203
|
3.7
|
20.5
|
1.0
|
|
N
|
O:GLU204
|
3.7
|
15.6
|
1.0
|
|
ND2
|
V:ASN123
|
3.8
|
17.8
|
1.0
|
|
CG2
|
O:THR173
|
3.9
|
11.7
|
1.0
|
|
NZ
|
O:LYS175
|
4.0
|
14.4
|
1.0
|
|
NE2
|
O:HIS294
|
4.0
|
13.8
|
1.0
|
|
CA
|
O:ASP203
|
4.1
|
14.9
|
1.0
|
|
CB
|
O:ASP203
|
4.1
|
14.3
|
1.0
|
|
NZ
|
O:KCX201
|
4.2
|
13.4
|
1.0
|
|
O6
|
O:CAP477
|
4.2
|
17.9
|
1.0
|
|
OG1
|
O:THR173
|
4.3
|
17.5
|
1.0
|
|
C4
|
O:CAP477
|
4.3
|
15.6
|
1.0
|
|
CG
|
O:GLU204
|
4.3
|
13.8
|
1.0
|
|
C1
|
O:CAP477
|
4.4
|
19.8
|
1.0
|
|
C
|
O:ASP203
|
4.5
|
15.8
|
1.0
|
|
CB
|
O:GLU204
|
4.5
|
14.7
|
1.0
|
|
CD2
|
O:HIS294
|
4.7
|
12.0
|
1.0
|
|
CB
|
O:THR173
|
4.7
|
17.3
|
1.0
|
|
CA
|
O:GLU204
|
4.7
|
15.1
|
1.0
|
|
C5
|
O:CAP477
|
4.7
|
14.1
|
1.0
|
|
O1
|
O:CAP477
|
4.8
|
19.4
|
1.0
|
|
CE1
|
O:HIS294
|
5.0
|
15.4
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 1uzh
Go back to
Magnesium Binding Sites List in 1uzh
Magnesium binding site 7 out
of 8 in the A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Mg476
b:12.0
occ:1.00
|
OD1
|
R:ASP203
|
2.0
|
17.2
|
1.0
|
|
OQ2
|
R:KCX201
|
2.0
|
15.2
|
1.0
|
|
OE1
|
R:GLU204
|
2.0
|
16.7
|
1.0
|
|
O3
|
R:CAP477
|
2.3
|
17.9
|
1.0
|
|
O7
|
R:CAP477
|
2.3
|
16.6
|
1.0
|
|
O2
|
R:CAP477
|
2.3
|
17.7
|
1.0
|
|
C2
|
R:CAP477
|
3.0
|
16.4
|
1.0
|
|
C
|
R:CAP477
|
3.0
|
17.1
|
1.0
|
|
CX
|
R:KCX201
|
3.1
|
15.9
|
1.0
|
|
CD
|
R:GLU204
|
3.1
|
15.7
|
1.0
|
|
CG
|
R:ASP203
|
3.1
|
17.7
|
1.0
|
|
C3
|
R:CAP477
|
3.2
|
16.7
|
1.0
|
|
OQ1
|
R:KCX201
|
3.3
|
14.8
|
1.0
|
|
OE2
|
R:GLU204
|
3.5
|
18.0
|
1.0
|
|
NZ
|
R:LYS177
|
3.7
|
15.2
|
1.0
|
|
N
|
R:GLU204
|
3.7
|
15.5
|
1.0
|
|
OD2
|
R:ASP203
|
3.8
|
20.4
|
1.0
|
|
ND2
|
H:ASN123
|
3.8
|
17.6
|
1.0
|
|
CG2
|
R:THR173
|
4.0
|
11.7
|
1.0
|
|
NZ
|
R:LYS175
|
4.0
|
14.2
|
1.0
|
|
NE2
|
R:HIS294
|
4.0
|
13.6
|
1.0
|
|
CA
|
R:ASP203
|
4.1
|
14.8
|
1.0
|
|
CB
|
R:ASP203
|
4.2
|
14.3
|
1.0
|
|
NZ
|
R:KCX201
|
4.2
|
13.3
|
1.0
|
|
O6
|
R:CAP477
|
4.3
|
19.0
|
1.0
|
|
OG1
|
R:THR173
|
4.3
|
17.4
|
1.0
|
|
CG
|
R:GLU204
|
4.3
|
13.4
|
1.0
|
|
C4
|
R:CAP477
|
4.3
|
22.4
|
1.0
|
|
C1
|
R:CAP477
|
4.4
|
15.5
|
1.0
|
|
C
|
R:ASP203
|
4.4
|
15.8
|
1.0
|
|
CB
|
R:GLU204
|
4.5
|
15.0
|
1.0
|
|
CD2
|
R:HIS294
|
4.6
|
12.4
|
1.0
|
|
CB
|
R:THR173
|
4.7
|
17.3
|
1.0
|
|
CA
|
R:GLU204
|
4.7
|
15.2
|
1.0
|
|
C5
|
R:CAP477
|
4.8
|
20.1
|
1.0
|
|
O1
|
R:CAP477
|
4.8
|
15.9
|
1.0
|
|
CE1
|
R:HIS294
|
4.9
|
15.7
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 1uzh
Go back to
Magnesium Binding Sites List in 1uzh
Magnesium binding site 8 out
of 8 in the A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme
 Mono view
 Stereo pair view
|
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of A Chimeric Chlamydomonas, Synechococcus Rubisco Enzyme within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
V:Mg476
b:16.3
occ:1.00
|
OQ2
|
V:KCX201
|
2.0
|
14.8
|
1.0
|
|
OD1
|
V:ASP203
|
2.0
|
17.3
|
1.0
|
|
O3
|
V:CAP477
|
2.1
|
17.0
|
1.0
|
|
O2
|
V:CAP477
|
2.1
|
21.2
|
1.0
|
|
O7
|
V:CAP477
|
2.1
|
20.4
|
1.0
|
|
OE1
|
V:GLU204
|
2.1
|
16.8
|
1.0
|
|
C2
|
V:CAP477
|
2.7
|
23.7
|
1.0
|
|
C
|
V:CAP477
|
2.8
|
21.0
|
1.0
|
|
C3
|
V:CAP477
|
2.9
|
17.9
|
1.0
|
|
CX
|
V:KCX201
|
3.0
|
16.2
|
1.0
|
|
CD
|
V:GLU204
|
3.2
|
16.0
|
1.0
|
|
CG
|
V:ASP203
|
3.2
|
17.6
|
1.0
|
|
OQ1
|
V:KCX201
|
3.2
|
14.9
|
1.0
|
|
OE2
|
V:GLU204
|
3.6
|
17.9
|
1.0
|
|
NZ
|
V:LYS177
|
3.8
|
15.1
|
1.0
|
|
OD2
|
V:ASP203
|
3.8
|
20.6
|
1.0
|
|
N
|
V:GLU204
|
3.8
|
15.6
|
1.0
|
|
ND2
|
O:ASN123
|
3.9
|
17.9
|
1.0
|
|
CG2
|
V:THR173
|
3.9
|
12.0
|
1.0
|
|
NZ
|
V:LYS175
|
4.0
|
14.3
|
1.0
|
|
NE2
|
V:HIS294
|
4.0
|
14.2
|
1.0
|
|
O6
|
V:CAP477
|
4.1
|
18.7
|
1.0
|
|
C4
|
V:CAP477
|
4.1
|
23.2
|
1.0
|
|
NZ
|
V:KCX201
|
4.2
|
13.6
|
1.0
|
|
CA
|
V:ASP203
|
4.2
|
14.9
|
1.0
|
|
C1
|
V:CAP477
|
4.2
|
20.2
|
1.0
|
|
OG1
|
V:THR173
|
4.2
|
17.4
|
1.0
|
|
CB
|
V:ASP203
|
4.2
|
14.5
|
1.0
|
|
CG
|
V:GLU204
|
4.4
|
13.7
|
1.0
|
|
C
|
V:ASP203
|
4.6
|
16.1
|
1.0
|
|
CB
|
V:THR173
|
4.6
|
17.2
|
1.0
|
|
CB
|
V:GLU204
|
4.6
|
14.8
|
1.0
|
|
C5
|
V:CAP477
|
4.6
|
18.0
|
1.0
|
|
CD2
|
V:HIS294
|
4.6
|
12.2
|
1.0
|
|
O1
|
V:CAP477
|
4.7
|
17.8
|
1.0
|
|
CA
|
V:GLU204
|
4.8
|
14.8
|
1.0
|
|
CE1
|
V:HIS294
|
5.0
|
15.3
|
1.0
|
|
Reference:
S.Karkehabadi,
S.R.Peddi,
M.Anwaruzzaman,
T.C.Taylor,
A.Cederlund,
T.Genkov,
I.Andersson,
R.J.Spreitzer.
Chimeric Small Subunits Influence Catalysis Without Causing Global Conformational Changes in the Crystal Structure of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Biochemistry V. 44 9851 2005.
ISSN: ISSN 0006-2960
PubMed: 16026157
DOI: 10.1021/BI050537V
Page generated: Tue Aug 13 14:56:49 2024
|
