Copper in PDB 7vvr: Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K
Enzymatic activity of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K
All present enzymatic activity of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K:
7.1.1.9;
Protein crystallography data
The structure of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K, PDB code: 7vvr
was solved by
A.Shimada,
T.Tsukihara,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
39.95 /
1.65
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
182.307,
204.706,
177.379,
90,
90,
90
|
R / Rfree (%)
|
15.2 /
17.6
|
Other elements in 7vvr:
The structure of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K
(pdb code 7vvr). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K, PDB code: 7vvr:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 7vvr
Go back to
Copper Binding Sites List in 7vvr
Copper binding site 1 out
of 6 in the Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:21.7
occ:1.00
|
N
|
A:CYN606
|
2.0
|
22.0
|
1.0
|
NE2
|
A:HIS291
|
2.0
|
20.9
|
1.0
|
ND1
|
A:HIS240
|
2.0
|
19.9
|
1.0
|
NE2
|
A:HIS290
|
2.1
|
22.5
|
1.0
|
CE1
|
A:HIS291
|
2.9
|
20.2
|
1.0
|
CE1
|
A:HIS240
|
3.0
|
20.7
|
1.0
|
CD2
|
A:HIS291
|
3.0
|
21.1
|
1.0
|
CE1
|
A:HIS290
|
3.0
|
20.2
|
1.0
|
CG
|
A:HIS240
|
3.1
|
19.6
|
1.0
|
C
|
A:CYN606
|
3.2
|
21.7
|
1.0
|
CD2
|
A:HIS290
|
3.2
|
24.0
|
1.0
|
CB
|
A:HIS240
|
3.5
|
20.4
|
1.0
|
CA
|
A:HIS240
|
3.9
|
21.2
|
1.0
|
ND1
|
A:HIS291
|
4.0
|
19.5
|
1.0
|
CG
|
A:HIS291
|
4.1
|
19.7
|
1.0
|
NE2
|
A:HIS240
|
4.1
|
19.4
|
1.0
|
CD2
|
A:HIS240
|
4.2
|
19.9
|
1.0
|
ND1
|
A:HIS290
|
4.2
|
22.2
|
1.0
|
CG
|
A:HIS290
|
4.3
|
21.6
|
1.0
|
CG2
|
A:VAL243
|
4.6
|
21.2
|
1.0
|
NA
|
A:HEA602
|
4.6
|
23.0
|
1.0
|
C1A
|
A:HEA602
|
4.7
|
22.3
|
1.0
|
N
|
A:HIS240
|
4.8
|
20.8
|
1.0
|
C4A
|
A:HEA602
|
4.9
|
20.7
|
1.0
|
FE
|
A:HEA602
|
5.0
|
23.1
|
1.0
|
C2A
|
A:HEA602
|
5.0
|
22.1
|
1.0
|
CG1
|
A:VAL243
|
5.0
|
22.1
|
1.0
|
|
Copper binding site 2 out
of 6 in 7vvr
Go back to
Copper Binding Sites List in 7vvr
Copper binding site 2 out
of 6 in the Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu302
b:24.0
occ:1.00
|
CU1
|
B:CUA302
|
0.0
|
24.0
|
1.0
|
ND1
|
B:HIS161
|
2.1
|
25.6
|
1.0
|
SG
|
B:CYS196
|
2.3
|
25.3
|
1.0
|
SG
|
B:CYS200
|
2.4
|
23.6
|
1.0
|
SD
|
B:MET207
|
2.4
|
25.6
|
1.0
|
CU2
|
B:CUA302
|
2.5
|
23.4
|
1.0
|
CE1
|
B:HIS161
|
3.0
|
25.6
|
1.0
|
CG
|
B:HIS161
|
3.2
|
22.1
|
1.0
|
CE
|
B:MET207
|
3.2
|
24.0
|
1.0
|
CB
|
B:CYS200
|
3.2
|
24.1
|
1.0
|
CB
|
B:CYS196
|
3.4
|
24.7
|
1.0
|
CG
|
B:MET207
|
3.4
|
23.4
|
1.0
|
CB
|
B:HIS161
|
3.6
|
21.5
|
1.0
|
NE2
|
B:HIS161
|
4.2
|
23.0
|
1.0
|
CA
|
B:HIS161
|
4.2
|
21.5
|
1.0
|
O
|
B:GLU198
|
4.3
|
26.1
|
1.0
|
CD2
|
B:HIS161
|
4.3
|
22.2
|
1.0
|
ND1
|
B:HIS204
|
4.4
|
22.4
|
1.0
|
CD1
|
B:TRP104
|
4.5
|
24.9
|
1.0
|
CA
|
B:CYS200
|
4.7
|
22.5
|
1.0
|
O
|
B:HIS102
|
4.7
|
26.1
|
1.0
|
CA
|
B:HIS204
|
4.7
|
23.7
|
1.0
|
O
|
B:LEU160
|
4.8
|
23.1
|
1.0
|
CA
|
B:CYS196
|
4.8
|
23.6
|
1.0
|
CB
|
B:MET207
|
4.8
|
25.5
|
1.0
|
|
Copper binding site 3 out
of 6 in 7vvr
Go back to
Copper Binding Sites List in 7vvr
Copper binding site 3 out
of 6 in the Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu302
b:23.4
occ:1.00
|
CU2
|
B:CUA302
|
0.0
|
23.4
|
1.0
|
ND1
|
B:HIS204
|
2.0
|
22.4
|
1.0
|
SG
|
B:CYS200
|
2.2
|
23.6
|
1.0
|
SG
|
B:CYS196
|
2.3
|
25.3
|
1.0
|
CU1
|
B:CUA302
|
2.5
|
24.0
|
1.0
|
O
|
B:GLU198
|
2.7
|
26.1
|
1.0
|
CE1
|
B:HIS204
|
2.9
|
24.2
|
1.0
|
CG
|
B:HIS204
|
3.1
|
24.2
|
1.0
|
CB
|
B:CYS196
|
3.3
|
24.7
|
1.0
|
CB
|
B:CYS200
|
3.3
|
24.1
|
1.0
|
CB
|
B:HIS204
|
3.5
|
23.3
|
1.0
|
CA
|
B:HIS204
|
3.5
|
23.7
|
1.0
|
C
|
B:GLU198
|
3.7
|
23.1
|
1.0
|
N
|
B:CYS200
|
3.7
|
23.8
|
1.0
|
O
|
B:HIS204
|
3.8
|
25.8
|
1.0
|
NE2
|
B:HIS204
|
4.0
|
23.9
|
1.0
|
CA
|
B:CYS200
|
4.1
|
22.5
|
1.0
|
CD2
|
B:HIS204
|
4.1
|
22.9
|
1.0
|
ND1
|
B:HIS161
|
4.2
|
25.6
|
1.0
|
C
|
B:HIS204
|
4.2
|
24.7
|
1.0
|
C
|
B:CYS196
|
4.2
|
23.2
|
1.0
|
N
|
B:GLU198
|
4.2
|
23.0
|
1.0
|
O
|
B:CYS196
|
4.2
|
24.2
|
1.0
|
CA
|
B:ILE199
|
4.2
|
24.1
|
1.0
|
C
|
B:ILE199
|
4.3
|
23.6
|
1.0
|
SD
|
B:MET207
|
4.3
|
25.6
|
1.0
|
CA
|
B:CYS196
|
4.4
|
23.6
|
1.0
|
N
|
B:ILE199
|
4.4
|
22.2
|
1.0
|
CG
|
B:MET207
|
4.5
|
23.4
|
1.0
|
CA
|
B:GLU198
|
4.6
|
24.9
|
1.0
|
N
|
B:SER197
|
4.6
|
21.9
|
1.0
|
N
|
B:HIS204
|
4.7
|
25.3
|
1.0
|
CA
|
B:HIS161
|
4.9
|
21.5
|
1.0
|
CB
|
B:HIS161
|
5.0
|
21.5
|
1.0
|
CG
|
B:HIS161
|
5.0
|
22.1
|
1.0
|
|
Copper binding site 4 out
of 6 in 7vvr
Go back to
Copper Binding Sites List in 7vvr
Copper binding site 4 out
of 6 in the Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
N:Cu603
b:23.5
occ:1.00
|
ND1
|
N:HIS240
|
2.0
|
20.1
|
1.0
|
N
|
N:CYN606
|
2.0
|
26.4
|
1.0
|
NE2
|
N:HIS291
|
2.0
|
24.3
|
1.0
|
NE2
|
N:HIS290
|
2.1
|
25.8
|
1.0
|
CE1
|
N:HIS240
|
2.9
|
22.8
|
1.0
|
CE1
|
N:HIS291
|
2.9
|
21.5
|
1.0
|
CD2
|
N:HIS291
|
3.0
|
26.3
|
1.0
|
CG
|
N:HIS240
|
3.1
|
19.6
|
1.0
|
CE1
|
N:HIS290
|
3.1
|
25.3
|
1.0
|
C
|
N:CYN606
|
3.1
|
25.5
|
1.0
|
CD2
|
N:HIS290
|
3.1
|
23.4
|
1.0
|
CB
|
N:HIS240
|
3.4
|
21.6
|
1.0
|
CA
|
N:HIS240
|
3.9
|
21.1
|
1.0
|
ND1
|
N:HIS291
|
4.0
|
20.9
|
1.0
|
NE2
|
N:HIS240
|
4.1
|
21.5
|
1.0
|
CG
|
N:HIS291
|
4.1
|
22.8
|
1.0
|
CD2
|
N:HIS240
|
4.2
|
20.6
|
1.0
|
ND1
|
N:HIS290
|
4.2
|
23.4
|
1.0
|
CG
|
N:HIS290
|
4.3
|
23.3
|
1.0
|
CG2
|
N:VAL243
|
4.6
|
23.7
|
1.0
|
NA
|
N:HEA602
|
4.6
|
25.8
|
1.0
|
C1A
|
N:HEA602
|
4.8
|
25.7
|
1.0
|
N
|
N:HIS240
|
4.8
|
22.0
|
1.0
|
C4A
|
N:HEA602
|
4.8
|
22.1
|
1.0
|
FE
|
N:HEA602
|
5.0
|
24.9
|
1.0
|
CG1
|
N:VAL243
|
5.0
|
24.7
|
1.0
|
|
Copper binding site 5 out
of 6 in 7vvr
Go back to
Copper Binding Sites List in 7vvr
Copper binding site 5 out
of 6 in the Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu302
b:28.4
occ:1.00
|
CU1
|
O:CUA302
|
0.0
|
28.4
|
1.0
|
ND1
|
O:HIS161
|
2.1
|
27.9
|
1.0
|
SD
|
O:MET207
|
2.3
|
30.6
|
1.0
|
SG
|
O:CYS196
|
2.3
|
28.8
|
1.0
|
SG
|
O:CYS200
|
2.4
|
29.4
|
1.0
|
CU2
|
O:CUA302
|
2.5
|
27.9
|
1.0
|
CE1
|
O:HIS161
|
2.9
|
27.4
|
1.0
|
CE
|
O:MET207
|
3.1
|
29.8
|
1.0
|
CG
|
O:HIS161
|
3.2
|
25.6
|
1.0
|
CB
|
O:CYS200
|
3.3
|
26.3
|
1.0
|
CB
|
O:CYS196
|
3.4
|
30.9
|
1.0
|
CG
|
O:MET207
|
3.4
|
26.9
|
1.0
|
CB
|
O:HIS161
|
3.6
|
26.2
|
1.0
|
NE2
|
O:HIS161
|
4.1
|
27.6
|
1.0
|
CA
|
O:HIS161
|
4.2
|
27.1
|
1.0
|
O
|
O:GLU198
|
4.2
|
27.9
|
1.0
|
CD2
|
O:HIS161
|
4.2
|
28.1
|
1.0
|
CD1
|
O:TRP104
|
4.4
|
32.3
|
1.0
|
ND1
|
O:HIS204
|
4.4
|
28.9
|
1.0
|
O
|
O:HIS102
|
4.7
|
31.1
|
1.0
|
CA
|
O:CYS200
|
4.7
|
28.1
|
1.0
|
O
|
O:LEU160
|
4.7
|
27.4
|
1.0
|
CA
|
O:HIS204
|
4.7
|
30.2
|
1.0
|
CA
|
O:CYS196
|
4.8
|
25.8
|
1.0
|
CB
|
O:MET207
|
4.8
|
29.7
|
1.0
|
N
|
O:CYS200
|
5.0
|
27.4
|
1.0
|
|
Copper binding site 6 out
of 6 in 7vvr
Go back to
Copper Binding Sites List in 7vvr
Copper binding site 6 out
of 6 in the Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu302
b:27.9
occ:1.00
|
CU2
|
O:CUA302
|
0.0
|
27.9
|
1.0
|
ND1
|
O:HIS204
|
2.0
|
28.9
|
1.0
|
SG
|
O:CYS200
|
2.3
|
29.4
|
1.0
|
SG
|
O:CYS196
|
2.3
|
28.8
|
1.0
|
CU1
|
O:CUA302
|
2.5
|
28.4
|
1.0
|
O
|
O:GLU198
|
2.7
|
27.9
|
1.0
|
CE1
|
O:HIS204
|
2.9
|
26.1
|
1.0
|
CG
|
O:HIS204
|
3.1
|
28.4
|
1.0
|
CB
|
O:CYS196
|
3.2
|
30.9
|
1.0
|
CB
|
O:CYS200
|
3.4
|
26.3
|
1.0
|
CA
|
O:HIS204
|
3.5
|
30.2
|
1.0
|
CB
|
O:HIS204
|
3.6
|
27.0
|
1.0
|
N
|
O:CYS200
|
3.7
|
27.4
|
1.0
|
C
|
O:GLU198
|
3.7
|
26.4
|
1.0
|
O
|
O:HIS204
|
3.8
|
29.9
|
1.0
|
NE2
|
O:HIS204
|
4.0
|
26.7
|
1.0
|
ND1
|
O:HIS161
|
4.1
|
27.9
|
1.0
|
CA
|
O:CYS200
|
4.2
|
28.1
|
1.0
|
C
|
O:HIS204
|
4.2
|
29.2
|
1.0
|
CD2
|
O:HIS204
|
4.2
|
26.3
|
1.0
|
C
|
O:CYS196
|
4.2
|
28.6
|
1.0
|
N
|
O:GLU198
|
4.2
|
27.2
|
1.0
|
O
|
O:CYS196
|
4.2
|
28.4
|
1.0
|
CA
|
O:ILE199
|
4.3
|
27.5
|
1.0
|
C
|
O:ILE199
|
4.3
|
27.2
|
1.0
|
SD
|
O:MET207
|
4.3
|
30.6
|
1.0
|
CA
|
O:CYS196
|
4.3
|
25.8
|
1.0
|
N
|
O:ILE199
|
4.4
|
25.7
|
1.0
|
CG
|
O:MET207
|
4.5
|
26.9
|
1.0
|
N
|
O:SER197
|
4.6
|
27.5
|
1.0
|
CA
|
O:GLU198
|
4.6
|
29.0
|
1.0
|
N
|
O:HIS204
|
4.7
|
29.5
|
1.0
|
CA
|
O:HIS161
|
4.9
|
27.1
|
1.0
|
CB
|
O:HIS161
|
5.0
|
26.2
|
1.0
|
|
Reference:
A.Shimada,
T.Tsukihara.
Bovine Cytochrome C Oxidese in Cn-Bound Mixed Valence State at 50 K To Be Published.
Page generated: Wed Jul 31 09:18:09 2024
|