Copper in PDB 7xmb: Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113
Enzymatic activity of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113
All present enzymatic activity of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113:
7.1.1.9;
Protein crystallography data
The structure of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113, PDB code: 7xmb
was solved by
Y.Nishida,
K.Shinzawa-Itoh,
N.Mizuno,
T.Kumasaka,
S.Yoshikawa,
T.Tsukihara,
Y.Shintani,
S.Takashima,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.98 /
2.20
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
182.097,
204.337,
177.933,
90,
90,
90
|
R / Rfree (%)
|
17.8 /
20.4
|
Other elements in 7xmb:
The structure of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113 also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113
(pdb code 7xmb). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113, PDB code: 7xmb:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 7xmb
Go back to
Copper Binding Sites List in 7xmb
Copper binding site 1 out
of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:19.6
occ:1.00
|
NE2
|
A:HIS290
|
2.0
|
25.6
|
1.0
|
NE2
|
A:HIS291
|
2.0
|
26.8
|
1.0
|
ND1
|
A:HIS240
|
2.2
|
28.1
|
1.0
|
O2
|
A:PER606
|
2.2
|
46.0
|
1.0
|
O1
|
A:PER606
|
2.6
|
54.5
|
1.0
|
CE1
|
A:HIS291
|
2.9
|
22.7
|
1.0
|
CE1
|
A:HIS290
|
2.9
|
20.9
|
1.0
|
CD2
|
A:HIS291
|
3.0
|
20.3
|
1.0
|
CD2
|
A:HIS290
|
3.1
|
24.6
|
1.0
|
CG
|
A:HIS240
|
3.1
|
46.4
|
1.0
|
CB
|
A:HIS240
|
3.2
|
15.0
|
1.0
|
CE1
|
A:HIS240
|
3.3
|
31.3
|
1.0
|
ND1
|
A:HIS291
|
3.9
|
18.2
|
1.0
|
CA
|
A:HIS240
|
3.9
|
24.2
|
1.0
|
CG
|
A:HIS291
|
4.0
|
21.8
|
1.0
|
ND1
|
A:HIS290
|
4.1
|
21.1
|
1.0
|
CG
|
A:HIS290
|
4.2
|
24.2
|
1.0
|
CD2
|
A:HIS240
|
4.3
|
21.5
|
1.0
|
NE2
|
A:HIS240
|
4.4
|
40.7
|
1.0
|
NA
|
A:HEA602
|
4.5
|
22.7
|
1.0
|
C1A
|
A:HEA602
|
4.7
|
22.9
|
1.0
|
N
|
A:HIS240
|
4.7
|
16.6
|
1.0
|
C4A
|
A:HEA602
|
4.8
|
24.8
|
1.0
|
CG2
|
A:VAL243
|
5.0
|
21.5
|
1.0
|
FE
|
A:HEA602
|
5.0
|
21.1
|
1.0
|
|
Copper binding site 2 out
of 6 in 7xmb
Go back to
Copper Binding Sites List in 7xmb
Copper binding site 2 out
of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu601
b:19.8
occ:1.00
|
CU1
|
B:CUA601
|
0.0
|
19.8
|
1.0
|
ND1
|
B:HIS161
|
2.0
|
23.5
|
1.0
|
SG
|
B:CYS200
|
2.3
|
23.9
|
1.0
|
SG
|
B:CYS196
|
2.3
|
24.7
|
1.0
|
SD
|
B:MET207
|
2.4
|
30.1
|
1.0
|
CU2
|
B:CUA601
|
2.4
|
21.0
|
1.0
|
CE1
|
B:HIS161
|
2.8
|
19.3
|
1.0
|
CE
|
B:MET207
|
3.0
|
30.0
|
1.0
|
CG
|
B:HIS161
|
3.2
|
26.1
|
1.0
|
CB
|
B:CYS200
|
3.3
|
24.9
|
1.0
|
CB
|
B:CYS196
|
3.4
|
34.4
|
1.0
|
CG
|
B:MET207
|
3.6
|
27.0
|
1.0
|
CB
|
B:HIS161
|
3.6
|
25.4
|
1.0
|
NE2
|
B:HIS161
|
4.0
|
22.3
|
1.0
|
CD2
|
B:HIS161
|
4.2
|
13.9
|
1.0
|
O
|
B:GLU198
|
4.2
|
28.0
|
1.0
|
CA
|
B:HIS161
|
4.3
|
18.3
|
1.0
|
ND1
|
B:HIS204
|
4.4
|
31.1
|
1.0
|
O
|
B:HIS102
|
4.5
|
28.0
|
1.0
|
O
|
B:LEU160
|
4.7
|
26.8
|
1.0
|
CD1
|
B:TRP104
|
4.7
|
21.4
|
1.0
|
CA
|
B:CYS200
|
4.7
|
35.0
|
1.0
|
CA
|
B:CYS196
|
4.8
|
23.9
|
1.0
|
O
|
B:HIS204
|
4.9
|
19.0
|
1.0
|
CA
|
B:HIS204
|
4.9
|
25.2
|
1.0
|
CB
|
B:MET207
|
4.9
|
24.2
|
1.0
|
|
Copper binding site 3 out
of 6 in 7xmb
Go back to
Copper Binding Sites List in 7xmb
Copper binding site 3 out
of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu601
b:21.0
occ:1.00
|
CU2
|
B:CUA601
|
0.0
|
21.0
|
1.0
|
ND1
|
B:HIS204
|
2.0
|
31.1
|
1.0
|
SG
|
B:CYS196
|
2.3
|
24.7
|
1.0
|
SG
|
B:CYS200
|
2.3
|
23.9
|
1.0
|
CU1
|
B:CUA601
|
2.4
|
19.8
|
1.0
|
O
|
B:GLU198
|
2.6
|
28.0
|
1.0
|
CE1
|
B:HIS204
|
2.7
|
33.8
|
1.0
|
CG
|
B:HIS204
|
3.2
|
37.2
|
1.0
|
CB
|
B:CYS196
|
3.3
|
34.4
|
1.0
|
CB
|
B:CYS200
|
3.4
|
24.9
|
1.0
|
C
|
B:GLU198
|
3.6
|
36.0
|
1.0
|
CA
|
B:HIS204
|
3.7
|
25.2
|
1.0
|
N
|
B:CYS200
|
3.7
|
25.2
|
1.0
|
O
|
B:HIS204
|
3.7
|
19.0
|
1.0
|
CB
|
B:HIS204
|
3.7
|
21.8
|
1.0
|
NE2
|
B:HIS204
|
3.9
|
28.4
|
1.0
|
ND1
|
B:HIS161
|
4.1
|
23.5
|
1.0
|
CD2
|
B:HIS204
|
4.1
|
26.6
|
1.0
|
CA
|
B:CYS200
|
4.2
|
35.0
|
1.0
|
C
|
B:HIS204
|
4.2
|
29.2
|
1.0
|
N
|
B:GLU198
|
4.2
|
25.9
|
1.0
|
SD
|
B:MET207
|
4.2
|
30.1
|
1.0
|
C
|
B:ILE199
|
4.3
|
33.4
|
1.0
|
C
|
B:CYS196
|
4.3
|
25.5
|
1.0
|
CA
|
B:ILE199
|
4.3
|
30.4
|
1.0
|
O
|
B:CYS196
|
4.4
|
23.5
|
1.0
|
CA
|
B:CYS196
|
4.4
|
23.9
|
1.0
|
N
|
B:ILE199
|
4.4
|
23.2
|
1.0
|
CA
|
B:GLU198
|
4.5
|
24.9
|
1.0
|
CG
|
B:MET207
|
4.6
|
27.0
|
1.0
|
N
|
B:SER197
|
4.7
|
23.3
|
1.0
|
CE1
|
B:HIS161
|
4.9
|
19.3
|
1.0
|
N
|
B:HIS204
|
4.9
|
28.8
|
1.0
|
CA
|
B:HIS161
|
5.0
|
18.3
|
1.0
|
CG
|
B:HIS161
|
5.0
|
26.1
|
1.0
|
|
Copper binding site 4 out
of 6 in 7xmb
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Copper Binding Sites List in 7xmb
Copper binding site 4 out
of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
N:Cu603
b:20.8
occ:1.00
|
NE2
|
N:HIS290
|
2.0
|
30.3
|
1.0
|
NE2
|
N:HIS291
|
2.0
|
25.9
|
1.0
|
O2
|
N:PER606
|
2.2
|
50.4
|
1.0
|
ND1
|
N:HIS240
|
2.2
|
34.2
|
1.0
|
O1
|
N:PER606
|
2.5
|
61.2
|
1.0
|
CE1
|
N:HIS291
|
2.9
|
27.9
|
1.0
|
CE1
|
N:HIS290
|
2.9
|
24.7
|
1.0
|
CD2
|
N:HIS291
|
3.0
|
22.8
|
1.0
|
CD2
|
N:HIS290
|
3.1
|
30.6
|
1.0
|
CG
|
N:HIS240
|
3.1
|
43.9
|
1.0
|
CB
|
N:HIS240
|
3.3
|
17.3
|
1.0
|
CE1
|
N:HIS240
|
3.3
|
30.0
|
1.0
|
ND1
|
N:HIS291
|
3.9
|
27.7
|
1.0
|
CA
|
N:HIS240
|
4.0
|
47.9
|
1.0
|
CG
|
N:HIS291
|
4.0
|
27.6
|
1.0
|
ND1
|
N:HIS290
|
4.1
|
27.6
|
1.0
|
CG
|
N:HIS290
|
4.2
|
24.7
|
1.0
|
CD2
|
N:HIS240
|
4.3
|
20.8
|
1.0
|
NE2
|
N:HIS240
|
4.4
|
43.3
|
1.0
|
NA
|
N:HEA602
|
4.5
|
23.1
|
1.0
|
C1A
|
N:HEA602
|
4.6
|
23.4
|
1.0
|
N
|
N:HIS240
|
4.7
|
15.5
|
1.0
|
C4A
|
N:HEA602
|
4.8
|
28.7
|
1.0
|
CG2
|
N:VAL243
|
4.9
|
23.3
|
1.0
|
C2A
|
N:HEA602
|
5.0
|
32.8
|
1.0
|
O
|
N:HOH883
|
5.0
|
56.6
|
1.0
|
CHA
|
N:HEA602
|
5.0
|
19.6
|
1.0
|
FE
|
N:HEA602
|
5.0
|
22.6
|
1.0
|
|
Copper binding site 5 out
of 6 in 7xmb
Go back to
Copper Binding Sites List in 7xmb
Copper binding site 5 out
of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu601
b:23.4
occ:1.00
|
CU1
|
O:CUA601
|
0.0
|
23.4
|
1.0
|
ND1
|
O:HIS161
|
2.0
|
27.3
|
1.0
|
SG
|
O:CYS200
|
2.3
|
30.1
|
1.0
|
SG
|
O:CYS196
|
2.3
|
28.9
|
1.0
|
SD
|
O:MET207
|
2.4
|
35.2
|
1.0
|
CU2
|
O:CUA601
|
2.4
|
22.8
|
1.0
|
CE1
|
O:HIS161
|
2.8
|
23.4
|
1.0
|
CE
|
O:MET207
|
3.0
|
26.1
|
1.0
|
CG
|
O:HIS161
|
3.2
|
28.6
|
1.0
|
CB
|
O:CYS200
|
3.3
|
32.1
|
1.0
|
CB
|
O:CYS196
|
3.4
|
34.6
|
1.0
|
CG
|
O:MET207
|
3.6
|
29.9
|
1.0
|
CB
|
O:HIS161
|
3.6
|
37.0
|
1.0
|
NE2
|
O:HIS161
|
4.0
|
30.1
|
1.0
|
CD2
|
O:HIS161
|
4.2
|
21.1
|
1.0
|
O
|
O:GLU198
|
4.2
|
30.3
|
1.0
|
CA
|
O:HIS161
|
4.3
|
29.9
|
1.0
|
ND1
|
O:HIS204
|
4.4
|
22.8
|
1.0
|
O
|
O:HIS102
|
4.5
|
29.0
|
1.0
|
CD1
|
O:TRP104
|
4.6
|
22.1
|
1.0
|
O
|
O:LEU160
|
4.6
|
28.4
|
1.0
|
CA
|
O:CYS200
|
4.7
|
22.4
|
1.0
|
O
|
O:HIS204
|
4.8
|
26.6
|
1.0
|
CA
|
O:CYS196
|
4.8
|
36.5
|
1.0
|
CB
|
O:MET207
|
4.9
|
24.1
|
1.0
|
CA
|
O:HIS204
|
4.9
|
27.6
|
1.0
|
|
Copper binding site 6 out
of 6 in 7xmb
Go back to
Copper Binding Sites List in 7xmb
Copper binding site 6 out
of 6 in the Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Crystal Structure of Bovine Heart Cytochrome C Oxidase, the Structure Complexed with An Allosteric Inhibitor T113 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu601
b:22.8
occ:1.00
|
CU2
|
O:CUA601
|
0.0
|
22.8
|
1.0
|
ND1
|
O:HIS204
|
2.0
|
22.8
|
1.0
|
SG
|
O:CYS200
|
2.3
|
30.1
|
1.0
|
SG
|
O:CYS196
|
2.3
|
28.9
|
1.0
|
CU1
|
O:CUA601
|
2.4
|
23.4
|
1.0
|
O
|
O:GLU198
|
2.6
|
30.3
|
1.0
|
CE1
|
O:HIS204
|
2.7
|
41.7
|
1.0
|
CG
|
O:HIS204
|
3.2
|
34.6
|
1.0
|
CB
|
O:CYS196
|
3.3
|
34.6
|
1.0
|
CB
|
O:CYS200
|
3.4
|
32.1
|
1.0
|
C
|
O:GLU198
|
3.6
|
37.5
|
1.0
|
O
|
O:HIS204
|
3.7
|
26.6
|
1.0
|
CA
|
O:HIS204
|
3.7
|
27.6
|
1.0
|
N
|
O:CYS200
|
3.7
|
26.5
|
1.0
|
CB
|
O:HIS204
|
3.8
|
31.2
|
1.0
|
NE2
|
O:HIS204
|
3.9
|
23.8
|
1.0
|
ND1
|
O:HIS161
|
4.1
|
27.3
|
1.0
|
C
|
O:HIS204
|
4.1
|
28.1
|
1.0
|
CA
|
O:CYS200
|
4.1
|
22.4
|
1.0
|
CD2
|
O:HIS204
|
4.2
|
23.1
|
1.0
|
N
|
O:GLU198
|
4.2
|
26.1
|
1.0
|
SD
|
O:MET207
|
4.2
|
35.2
|
1.0
|
C
|
O:ILE199
|
4.2
|
37.3
|
1.0
|
C
|
O:CYS196
|
4.3
|
36.7
|
1.0
|
CA
|
O:ILE199
|
4.3
|
31.5
|
1.0
|
O
|
O:CYS196
|
4.4
|
27.8
|
1.0
|
N
|
O:ILE199
|
4.4
|
21.7
|
1.0
|
CA
|
O:CYS196
|
4.4
|
36.5
|
1.0
|
CA
|
O:GLU198
|
4.6
|
28.0
|
1.0
|
CG
|
O:MET207
|
4.6
|
29.9
|
1.0
|
N
|
O:SER197
|
4.7
|
30.0
|
1.0
|
CE1
|
O:HIS161
|
4.9
|
23.4
|
1.0
|
N
|
O:HIS204
|
4.9
|
39.1
|
1.0
|
CA
|
O:HIS161
|
5.0
|
29.9
|
1.0
|
CG
|
O:HIS161
|
5.0
|
28.6
|
1.0
|
|
Reference:
Y.Nishida,
S.Yanagisawa,
R.Morita,
H.Shigematsu,
K.Shinzawa-Itoh,
H.Yuki,
S.Ogasawara,
K.Shimuta,
T.Iwamoto,
C.Nakabayashi,
W.Matsumura,
H.Kato,
C.Gopalasingam,
T.Nagao,
T.Qaqorh,
Y.Takahashi,
S.Yamazaki,
K.Kamiya,
R.Harada,
N.Mizuno,
H.Takahashi,
Y.Akeda,
M.Ohnishi,
Y.Ishii,
T.Kumasaka,
T.Murata,
K.Muramoto,
T.Tosha,
Y.Shiro,
T.Honma,
Y.Shigeta,
M.Kubo,
S.Takashima,
Y.Shintani.
Identifying Antibiotics Based on Structural Differences in the Conserved Allostery From Mitochondrial Heme-Copper Oxidases. Nat Commun V. 13 7591 2022.
ISSN: ESSN 2041-1723
PubMed: 36481732
DOI: 10.1038/S41467-022-34771-Y
Page generated: Wed Jul 31 09:23:37 2024
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