Copper in PDB 3ag2: Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
All present enzymatic activity of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K:
1.9.3.1;
Protein crystallography data
The structure of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K, PDB code: 3ag2
was solved by
K.Muramoto,
K.Ohta,
K.Shinzawa-Itoh,
K.Kanda,
M.Taniguchi,
H.Nabekura,
E.Yamashita,
T.Tsukihara,
S.Yoshikawa,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
40.00 /
1.80
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
182.834,
206.933,
178.090,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.2 /
22.3
|
Other elements in 3ag2:
The structure of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
(pdb code 3ag2). 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 Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K, PDB code: 3ag2:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 3ag2
Go back to
Copper Binding Sites List in 3ag2
Copper binding site 1 out
of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu517
b:22.4
occ:1.00
|
NE2
|
A:HIS291
|
2.0
|
27.7
|
1.0
|
NE2
|
A:HIS290
|
2.0
|
21.8
|
1.0
|
ND1
|
A:HIS240
|
2.0
|
30.1
|
1.0
|
C
|
A:CMO520
|
2.4
|
25.8
|
1.0
|
O
|
A:CMO520
|
2.7
|
25.5
|
1.0
|
CE1
|
A:HIS291
|
2.9
|
22.8
|
1.0
|
CD2
|
A:HIS291
|
2.9
|
21.1
|
1.0
|
CE1
|
A:HIS290
|
3.0
|
26.0
|
1.0
|
CE1
|
A:HIS240
|
3.0
|
18.0
|
1.0
|
CD2
|
A:HIS290
|
3.0
|
19.5
|
1.0
|
CG
|
A:HIS240
|
3.2
|
24.9
|
1.0
|
CB
|
A:HIS240
|
3.6
|
21.0
|
1.0
|
ND1
|
A:HIS291
|
4.0
|
20.6
|
1.0
|
CG
|
A:HIS291
|
4.0
|
23.8
|
1.0
|
ND1
|
A:HIS290
|
4.1
|
23.2
|
1.0
|
CA
|
A:HIS240
|
4.2
|
18.3
|
1.0
|
NE2
|
A:HIS240
|
4.2
|
26.2
|
1.0
|
CG
|
A:HIS290
|
4.2
|
24.4
|
1.0
|
CD2
|
A:HIS240
|
4.3
|
33.2
|
1.0
|
NA
|
A:HEA516
|
4.3
|
26.2
|
1.0
|
C1A
|
A:HEA516
|
4.3
|
19.6
|
1.0
|
C4A
|
A:HEA516
|
4.4
|
15.9
|
1.0
|
C2A
|
A:HEA516
|
4.5
|
18.4
|
1.0
|
CG2
|
A:VAL243
|
4.7
|
21.5
|
1.0
|
C3A
|
A:HEA516
|
4.7
|
18.0
|
1.0
|
CHA
|
A:HEA516
|
4.9
|
20.4
|
1.0
|
FE
|
A:HEA516
|
5.0
|
22.6
|
1.0
|
|
Copper binding site 2 out
of 6 in 3ag2
Go back to
Copper Binding Sites List in 3ag2
Copper binding site 2 out
of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu228
b:24.7
occ:1.00
|
CU1
|
B:CUA228
|
0.0
|
24.7
|
1.0
|
ND1
|
B:HIS161
|
2.0
|
22.9
|
1.0
|
SG
|
B:CYS196
|
2.3
|
22.8
|
1.0
|
SG
|
B:CYS200
|
2.4
|
20.9
|
1.0
|
SD
|
B:MET207
|
2.4
|
24.7
|
1.0
|
CU2
|
B:CUA228
|
2.6
|
23.8
|
1.0
|
CE1
|
B:HIS161
|
2.9
|
20.1
|
1.0
|
CE
|
B:MET207
|
3.0
|
16.4
|
1.0
|
CG
|
B:HIS161
|
3.2
|
12.2
|
1.0
|
CB
|
B:CYS200
|
3.4
|
23.0
|
1.0
|
CB
|
B:CYS196
|
3.6
|
20.4
|
1.0
|
CB
|
B:HIS161
|
3.6
|
17.2
|
1.0
|
CG
|
B:MET207
|
3.6
|
26.3
|
1.0
|
O
|
B:GLU198
|
4.1
|
28.2
|
1.0
|
CA
|
B:HIS161
|
4.1
|
17.5
|
1.0
|
NE2
|
B:HIS161
|
4.1
|
19.8
|
1.0
|
CD2
|
B:HIS161
|
4.3
|
22.4
|
1.0
|
ND1
|
B:HIS204
|
4.5
|
29.0
|
1.0
|
CD1
|
B:TRP104
|
4.6
|
21.5
|
1.0
|
O
|
B:LEU160
|
4.7
|
22.9
|
1.0
|
O
|
B:HIS102
|
4.8
|
20.0
|
1.0
|
CA
|
B:CYS200
|
4.8
|
18.9
|
1.0
|
CA
|
B:HIS204
|
4.8
|
19.9
|
1.0
|
CA
|
B:CYS196
|
4.9
|
24.1
|
1.0
|
CB
|
B:MET207
|
5.0
|
23.4
|
1.0
|
N
|
B:SER162
|
5.0
|
21.7
|
1.0
|
O
|
B:HIS204
|
5.0
|
21.6
|
1.0
|
|
Copper binding site 3 out
of 6 in 3ag2
Go back to
Copper Binding Sites List in 3ag2
Copper binding site 3 out
of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu228
b:23.8
occ:1.00
|
CU2
|
B:CUA228
|
0.0
|
23.8
|
1.0
|
ND1
|
B:HIS204
|
2.0
|
29.0
|
1.0
|
SG
|
B:CYS200
|
2.2
|
20.9
|
1.0
|
SG
|
B:CYS196
|
2.4
|
22.8
|
1.0
|
O
|
B:GLU198
|
2.4
|
28.2
|
1.0
|
CU1
|
B:CUA228
|
2.6
|
24.7
|
1.0
|
CE1
|
B:HIS204
|
2.9
|
24.5
|
1.0
|
CG
|
B:HIS204
|
3.1
|
24.0
|
1.0
|
CB
|
B:CYS196
|
3.4
|
20.4
|
1.0
|
CB
|
B:HIS204
|
3.5
|
20.6
|
1.0
|
C
|
B:GLU198
|
3.6
|
24.6
|
1.0
|
CA
|
B:HIS204
|
3.6
|
19.9
|
1.0
|
CB
|
B:CYS200
|
3.6
|
23.0
|
1.0
|
N
|
B:CYS200
|
3.7
|
23.1
|
1.0
|
O
|
B:HIS204
|
3.8
|
21.6
|
1.0
|
NE2
|
B:HIS204
|
4.1
|
23.7
|
1.0
|
C
|
B:HIS204
|
4.1
|
23.1
|
1.0
|
CD2
|
B:HIS204
|
4.2
|
23.8
|
1.0
|
ND1
|
B:HIS161
|
4.2
|
22.9
|
1.0
|
C
|
B:ILE199
|
4.2
|
25.3
|
1.0
|
N
|
B:GLU198
|
4.2
|
23.9
|
1.0
|
C
|
B:CYS196
|
4.2
|
20.1
|
1.0
|
CA
|
B:CYS200
|
4.2
|
18.9
|
1.0
|
O
|
B:CYS196
|
4.3
|
16.3
|
1.0
|
CA
|
B:ILE199
|
4.3
|
24.4
|
1.0
|
N
|
B:ILE199
|
4.3
|
24.1
|
1.0
|
SD
|
B:MET207
|
4.4
|
24.7
|
1.0
|
CA
|
B:CYS196
|
4.5
|
24.1
|
1.0
|
CA
|
B:GLU198
|
4.6
|
22.6
|
1.0
|
N
|
B:SER197
|
4.6
|
22.9
|
1.0
|
CG
|
B:MET207
|
4.8
|
26.3
|
1.0
|
N
|
B:HIS204
|
4.8
|
24.0
|
1.0
|
CA
|
B:HIS161
|
4.8
|
17.5
|
1.0
|
|
Copper binding site 4 out
of 6 in 3ag2
Go back to
Copper Binding Sites List in 3ag2
Copper binding site 4 out
of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
N:Cu517
b:29.1
occ:1.00
|
NE2
|
N:HIS290
|
1.9
|
30.0
|
1.0
|
NE2
|
N:HIS291
|
2.0
|
30.7
|
1.0
|
ND1
|
N:HIS240
|
2.0
|
30.8
|
1.0
|
C
|
N:CMO520
|
2.5
|
30.9
|
1.0
|
O
|
N:CMO520
|
2.6
|
30.1
|
1.0
|
CE1
|
N:HIS290
|
2.8
|
31.9
|
1.0
|
CE1
|
N:HIS240
|
2.9
|
24.5
|
1.0
|
CE1
|
N:HIS291
|
3.0
|
25.9
|
1.0
|
CD2
|
N:HIS291
|
3.0
|
27.2
|
1.0
|
CD2
|
N:HIS290
|
3.1
|
29.0
|
1.0
|
CG
|
N:HIS240
|
3.2
|
27.7
|
1.0
|
CB
|
N:HIS240
|
3.6
|
25.8
|
1.0
|
ND1
|
N:HIS290
|
4.0
|
29.6
|
1.0
|
ND1
|
N:HIS291
|
4.0
|
28.1
|
1.0
|
NE2
|
N:HIS240
|
4.1
|
29.0
|
1.0
|
CG
|
N:HIS291
|
4.1
|
32.4
|
1.0
|
CG
|
N:HIS290
|
4.1
|
29.4
|
1.0
|
CA
|
N:HIS240
|
4.1
|
25.1
|
1.0
|
CD2
|
N:HIS240
|
4.2
|
30.5
|
1.0
|
NA
|
N:HEA516
|
4.3
|
31.1
|
1.0
|
C1A
|
N:HEA516
|
4.4
|
29.0
|
1.0
|
C4A
|
N:HEA516
|
4.4
|
26.1
|
1.0
|
C2A
|
N:HEA516
|
4.6
|
28.5
|
1.0
|
C3A
|
N:HEA516
|
4.6
|
27.1
|
1.0
|
CG2
|
N:VAL243
|
4.8
|
24.1
|
1.0
|
CHA
|
N:HEA516
|
4.8
|
21.4
|
1.0
|
FE
|
N:HEA516
|
5.0
|
29.0
|
1.0
|
|
Copper binding site 5 out
of 6 in 3ag2
Go back to
Copper Binding Sites List in 3ag2
Copper binding site 5 out
of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu228
b:31.5
occ:1.00
|
CU1
|
O:CUA228
|
0.0
|
31.5
|
1.0
|
ND1
|
O:HIS161
|
2.0
|
30.8
|
1.0
|
SG
|
O:CYS196
|
2.3
|
30.8
|
1.0
|
SD
|
O:MET207
|
2.4
|
32.6
|
1.0
|
SG
|
O:CYS200
|
2.4
|
29.4
|
1.0
|
CU2
|
O:CUA228
|
2.5
|
31.7
|
1.0
|
CE1
|
O:HIS161
|
2.9
|
28.7
|
1.0
|
CG
|
O:HIS161
|
3.1
|
22.7
|
1.0
|
CE
|
O:MET207
|
3.2
|
20.8
|
1.0
|
CB
|
O:CYS200
|
3.3
|
30.6
|
1.0
|
CG
|
O:MET207
|
3.5
|
26.5
|
1.0
|
CB
|
O:CYS196
|
3.5
|
29.1
|
1.0
|
CB
|
O:HIS161
|
3.6
|
29.6
|
1.0
|
O
|
O:GLU198
|
4.0
|
31.7
|
1.0
|
NE2
|
O:HIS161
|
4.0
|
28.7
|
1.0
|
CD2
|
O:HIS161
|
4.2
|
30.4
|
1.0
|
CA
|
O:HIS161
|
4.3
|
29.8
|
1.0
|
CD1
|
O:TRP104
|
4.5
|
31.0
|
1.0
|
ND1
|
O:HIS204
|
4.5
|
35.9
|
1.0
|
O
|
O:HIS102
|
4.7
|
27.4
|
1.0
|
CA
|
O:CYS200
|
4.7
|
29.9
|
1.0
|
CA
|
O:HIS204
|
4.7
|
30.0
|
1.0
|
O
|
O:LEU160
|
4.8
|
30.5
|
1.0
|
CA
|
O:CYS196
|
4.9
|
30.2
|
1.0
|
CB
|
O:MET207
|
4.9
|
29.0
|
1.0
|
O
|
O:HIS204
|
5.0
|
30.5
|
1.0
|
N
|
O:CYS200
|
5.0
|
30.0
|
1.0
|
|
Copper binding site 6 out
of 6 in 3ag2
Go back to
Copper Binding Sites List in 3ag2
Copper binding site 6 out
of 6 in the Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Bovine Heart Cytochrome C Oxidase in the Carbon Monoxide-Bound Fully Reduced State at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu228
b:31.7
occ:1.00
|
CU2
|
O:CUA228
|
0.0
|
31.7
|
1.0
|
ND1
|
O:HIS204
|
2.0
|
35.9
|
1.0
|
SG
|
O:CYS200
|
2.3
|
29.4
|
1.0
|
SG
|
O:CYS196
|
2.3
|
30.8
|
1.0
|
O
|
O:GLU198
|
2.3
|
31.7
|
1.0
|
CU1
|
O:CUA228
|
2.5
|
31.5
|
1.0
|
CE1
|
O:HIS204
|
2.9
|
32.5
|
1.0
|
CG
|
O:HIS204
|
3.1
|
29.1
|
1.0
|
CB
|
O:CYS196
|
3.3
|
29.1
|
1.0
|
CB
|
O:CYS200
|
3.4
|
30.6
|
1.0
|
CB
|
O:HIS204
|
3.5
|
28.5
|
1.0
|
C
|
O:GLU198
|
3.5
|
28.4
|
1.0
|
CA
|
O:HIS204
|
3.5
|
30.0
|
1.0
|
N
|
O:CYS200
|
3.7
|
30.0
|
1.0
|
O
|
O:HIS204
|
3.8
|
30.5
|
1.0
|
NE2
|
O:HIS204
|
4.1
|
33.6
|
1.0
|
ND1
|
O:HIS161
|
4.1
|
30.8
|
1.0
|
CD2
|
O:HIS204
|
4.2
|
27.6
|
1.0
|
C
|
O:HIS204
|
4.2
|
30.1
|
1.0
|
N
|
O:GLU198
|
4.2
|
29.0
|
1.0
|
CA
|
O:CYS200
|
4.2
|
29.9
|
1.0
|
O
|
O:CYS196
|
4.2
|
29.4
|
1.0
|
C
|
O:ILE199
|
4.2
|
30.3
|
1.0
|
CA
|
O:ILE199
|
4.3
|
29.3
|
1.0
|
C
|
O:CYS196
|
4.3
|
30.1
|
1.0
|
N
|
O:ILE199
|
4.3
|
27.8
|
1.0
|
SD
|
O:MET207
|
4.4
|
32.6
|
1.0
|
CA
|
O:CYS196
|
4.4
|
30.2
|
1.0
|
CA
|
O:GLU198
|
4.5
|
30.0
|
1.0
|
CG
|
O:MET207
|
4.7
|
26.5
|
1.0
|
N
|
O:SER197
|
4.7
|
31.5
|
1.0
|
N
|
O:HIS204
|
4.7
|
30.4
|
1.0
|
CA
|
O:HIS161
|
4.9
|
29.8
|
1.0
|
CB
|
O:HIS161
|
4.9
|
29.6
|
1.0
|
CG
|
O:HIS161
|
4.9
|
22.7
|
1.0
|
CE1
|
O:HIS161
|
5.0
|
28.7
|
1.0
|
|
Reference:
K.Muramoto,
K.Ohta,
K.Shinzawa-Itoh,
K.Kanda,
M.Taniguchi,
H.Nabekura,
E.Yamashita,
T.Tsukihara,
S.Yoshikawa.
Bovine Cytochrome C Oxidase Structures Enable O2 Reduction with Minimization of Reactive Oxygens and Provide A Proton-Pumping Gate Proc.Natl.Acad.Sci.Usa V. 107 7740 2010.
ISSN: ISSN 0027-8424
PubMed: 20385840
DOI: 10.1073/PNAS.0910410107
Page generated: Wed Jul 31 00:36:17 2024
|