Copper in PDB 1zxi: Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans
Enzymatic activity of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans
All present enzymatic activity of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans:
1.2.99.2;
Protein crystallography data
The structure of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans, PDB code: 1zxi
was solved by
M.Resch,
H.Dobbek,
O.Meyer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
1.70
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
118.840,
131.320,
159.990,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.6 /
19.4
|
Other elements in 1zxi:
The structure of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans
(pdb code 1zxi). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the
Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans, PDB code: 1zxi:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 1zxi
Go back to
Copper Binding Sites List in 1zxi
Copper binding site 1 out
of 4 in the Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu3910
b:14.7
occ:0.20
|
OE2
|
B:GLU763
|
1.9
|
16.4
|
1.0
|
N
|
B:SER389
|
2.0
|
12.7
|
1.0
|
CU
|
B:CUM3920
|
2.2
|
15.7
|
0.6
|
OM2
|
B:CUM3920
|
2.7
|
15.3
|
1.0
|
N
|
B:CYS388
|
2.8
|
13.3
|
1.0
|
CA
|
B:SER389
|
2.8
|
13.4
|
1.0
|
CD
|
B:GLU763
|
2.9
|
13.3
|
1.0
|
C
|
B:CYS388
|
3.0
|
14.1
|
1.0
|
S
|
B:CUM3920
|
3.2
|
17.0
|
0.8
|
CA
|
B:CYS388
|
3.3
|
14.2
|
1.0
|
OE1
|
B:GLU763
|
3.4
|
14.9
|
1.0
|
C
|
B:ARG387
|
3.5
|
12.8
|
1.0
|
SG
|
B:CYS388
|
3.5
|
16.2
|
1.0
|
MO
|
B:CUM3920
|
3.5
|
13.0
|
1.0
|
N
|
B:PHE390
|
3.6
|
13.5
|
1.0
|
C
|
B:SER389
|
3.7
|
14.5
|
1.0
|
CA
|
B:ARG387
|
3.9
|
12.3
|
1.0
|
CB
|
B:CYS388
|
3.9
|
14.1
|
1.0
|
CB
|
B:SER389
|
4.0
|
14.4
|
1.0
|
O
|
B:CYS388
|
4.1
|
13.5
|
1.0
|
OG
|
B:SER389
|
4.1
|
14.0
|
1.0
|
CG
|
B:GLU763
|
4.2
|
13.1
|
1.0
|
N
|
B:GLY569
|
4.2
|
12.1
|
1.0
|
O
|
B:ARG387
|
4.3
|
12.4
|
1.0
|
CA
|
B:GLY569
|
4.3
|
12.2
|
1.0
|
N
|
B:ARG387
|
4.3
|
12.6
|
1.0
|
S8'
|
B:MCN3921
|
4.5
|
13.3
|
1.0
|
O
|
B:SER389
|
4.9
|
16.1
|
1.0
|
S7'
|
B:MCN3921
|
4.9
|
12.8
|
1.0
|
CA
|
B:PHE390
|
5.0
|
13.7
|
1.0
|
CB
|
B:GLU763
|
5.0
|
9.0
|
1.0
|
|
Copper binding site 2 out
of 4 in 1zxi
Go back to
Copper Binding Sites List in 1zxi
Copper binding site 2 out
of 4 in the Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu3920
b:15.7
occ:0.60
|
CU
|
B:CUM3920
|
0.0
|
15.7
|
0.6
|
CU
|
B:CU3910
|
2.2
|
14.7
|
0.2
|
S
|
B:CUM3920
|
2.3
|
17.0
|
0.8
|
SG
|
B:CYS388
|
2.4
|
16.2
|
1.0
|
N
|
B:CYS388
|
3.1
|
13.3
|
1.0
|
OM2
|
B:CUM3920
|
3.3
|
15.3
|
1.0
|
CB
|
B:CYS388
|
3.4
|
14.1
|
1.0
|
N
|
B:ALA385
|
3.4
|
11.7
|
1.0
|
CA
|
B:ALA385
|
3.5
|
11.2
|
1.0
|
N
|
B:SER389
|
3.5
|
12.7
|
1.0
|
CA
|
B:CYS388
|
3.6
|
14.2
|
1.0
|
C
|
B:ALA385
|
3.6
|
11.2
|
1.0
|
O
|
B:ALA385
|
3.7
|
11.9
|
1.0
|
OE2
|
B:GLU763
|
3.7
|
16.4
|
1.0
|
CG1
|
B:VAL384
|
3.8
|
17.1
|
1.0
|
MO
|
B:CUM3920
|
3.8
|
13.0
|
1.0
|
C
|
B:CYS388
|
3.9
|
14.1
|
1.0
|
C
|
B:VAL384
|
4.0
|
13.6
|
1.0
|
N
|
B:PHE390
|
4.2
|
13.5
|
1.0
|
C
|
B:ARG387
|
4.2
|
12.8
|
1.0
|
N
|
B:ARG387
|
4.2
|
12.6
|
1.0
|
N
|
B:TYR386
|
4.2
|
12.0
|
1.0
|
CA
|
B:ARG387
|
4.5
|
12.3
|
1.0
|
CA
|
B:SER389
|
4.5
|
13.4
|
1.0
|
CA
|
B:VAL384
|
4.6
|
13.2
|
1.0
|
O
|
B:VAL384
|
4.6
|
13.5
|
1.0
|
O
|
B:HOH4672
|
4.7
|
39.5
|
1.0
|
C
|
B:TYR386
|
4.8
|
12.8
|
1.0
|
CB
|
B:VAL384
|
4.8
|
15.8
|
1.0
|
C
|
B:SER389
|
4.9
|
14.5
|
1.0
|
OM1
|
B:CUM3920
|
4.9
|
16.0
|
1.0
|
CD
|
B:GLU763
|
5.0
|
13.3
|
1.0
|
O
|
B:CYS388
|
5.0
|
13.5
|
1.0
|
CB
|
B:ALA385
|
5.0
|
12.9
|
1.0
|
|
Copper binding site 3 out
of 4 in 1zxi
Go back to
Copper Binding Sites List in 1zxi
Copper binding site 3 out
of 4 in the Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Cu3911
b:15.0
occ:0.20
|
OE2
|
E:GLU763
|
1.8
|
14.7
|
1.0
|
N
|
E:SER389
|
2.2
|
13.1
|
1.0
|
CU
|
E:CUM3922
|
2.2
|
17.3
|
0.6
|
OM2
|
E:CUM3922
|
2.3
|
14.7
|
1.0
|
N
|
E:CYS388
|
2.9
|
13.8
|
1.0
|
CA
|
E:SER389
|
2.9
|
13.9
|
1.0
|
CD
|
E:GLU763
|
3.0
|
13.1
|
1.0
|
S
|
E:CUM3922
|
3.1
|
16.7
|
0.8
|
C
|
E:CYS388
|
3.1
|
14.2
|
1.0
|
MO
|
E:CUM3922
|
3.3
|
14.8
|
1.0
|
CA
|
E:CYS388
|
3.4
|
14.8
|
1.0
|
OE1
|
E:GLU763
|
3.4
|
12.3
|
1.0
|
SG
|
E:CYS388
|
3.6
|
19.4
|
1.0
|
C
|
E:ARG387
|
3.6
|
13.9
|
1.0
|
N
|
E:PHE390
|
3.7
|
15.7
|
1.0
|
C
|
E:SER389
|
3.8
|
14.3
|
1.0
|
CA
|
E:ARG387
|
4.0
|
13.2
|
1.0
|
CB
|
E:CYS388
|
4.0
|
13.9
|
1.0
|
N
|
E:GLY569
|
4.1
|
11.1
|
1.0
|
CB
|
E:SER389
|
4.2
|
14.5
|
1.0
|
CA
|
E:GLY569
|
4.2
|
11.5
|
1.0
|
CG
|
E:GLU763
|
4.2
|
12.8
|
1.0
|
OG
|
E:SER389
|
4.2
|
14.7
|
1.0
|
O
|
E:CYS388
|
4.3
|
13.6
|
1.0
|
S8'
|
E:MCN3923
|
4.3
|
13.0
|
1.0
|
N
|
E:ARG387
|
4.4
|
12.1
|
1.0
|
O
|
E:ARG387
|
4.5
|
13.7
|
1.0
|
OM1
|
E:CUM3922
|
4.8
|
16.3
|
1.0
|
S7'
|
E:MCN3923
|
4.8
|
13.2
|
1.0
|
O
|
E:SER389
|
5.0
|
16.6
|
1.0
|
|
Copper binding site 4 out
of 4 in 1zxi
Go back to
Copper Binding Sites List in 1zxi
Copper binding site 4 out
of 4 in the Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Reconstituted Co Dehydrogenase From Oligotropha Carboxidovorans within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Cu3922
b:17.3
occ:0.60
|
CU
|
E:CUM3922
|
0.0
|
17.3
|
0.6
|
CU
|
E:CU3911
|
2.2
|
15.0
|
0.2
|
S
|
E:CUM3922
|
2.3
|
16.7
|
0.8
|
SG
|
E:CYS388
|
2.4
|
19.4
|
1.0
|
N
|
E:CYS388
|
3.1
|
13.8
|
1.0
|
OM2
|
E:CUM3922
|
3.3
|
14.7
|
1.0
|
N
|
E:ALA385
|
3.3
|
14.3
|
1.0
|
CB
|
E:CYS388
|
3.3
|
13.9
|
1.0
|
CA
|
E:ALA385
|
3.4
|
14.1
|
1.0
|
C
|
E:ALA385
|
3.5
|
12.8
|
1.0
|
N
|
E:SER389
|
3.5
|
13.1
|
1.0
|
CA
|
E:CYS388
|
3.6
|
14.8
|
1.0
|
O
|
E:ALA385
|
3.7
|
12.6
|
1.0
|
CG1
|
E:VAL384
|
3.7
|
15.8
|
1.0
|
OE2
|
E:GLU763
|
3.7
|
14.7
|
1.0
|
MO
|
E:CUM3922
|
3.8
|
14.8
|
1.0
|
C
|
E:CYS388
|
3.9
|
14.2
|
1.0
|
C
|
E:VAL384
|
4.0
|
15.7
|
1.0
|
N
|
E:ARG387
|
4.2
|
12.1
|
1.0
|
N
|
E:TYR386
|
4.2
|
12.9
|
1.0
|
C
|
E:ARG387
|
4.2
|
13.9
|
1.0
|
N
|
E:PHE390
|
4.2
|
15.7
|
1.0
|
CA
|
E:ARG387
|
4.5
|
13.2
|
1.0
|
CA
|
E:SER389
|
4.6
|
13.9
|
1.0
|
CA
|
E:VAL384
|
4.6
|
15.3
|
1.0
|
O
|
E:VAL384
|
4.6
|
15.8
|
1.0
|
C
|
E:TYR386
|
4.7
|
13.0
|
1.0
|
CB
|
E:VAL384
|
4.8
|
15.8
|
1.0
|
OM1
|
E:CUM3922
|
4.9
|
16.3
|
1.0
|
CB
|
E:ALA385
|
4.9
|
13.3
|
1.0
|
O
|
E:CYS388
|
4.9
|
13.6
|
1.0
|
CD
|
E:GLU763
|
4.9
|
13.1
|
1.0
|
C
|
E:SER389
|
5.0
|
14.3
|
1.0
|
|
Reference:
M.Resch,
H.Dobbek,
O.Meyer.
Structural and Functional Reconstruction in Situ of the [Cusmoo(2)] Active Site of Carbon Monoxide Dehydrogenase From the Carbon Monoxide Oxidizing Eubacterium Oligotropha Carboxidovorans J.Biol.Inorg.Chem. V. 10 518 2005.
ISSN: ISSN 0949-8257
PubMed: 16091936
DOI: 10.1007/S00775-005-0006-4
Page generated: Tue Jul 30 23:06:27 2024
|