Copper in PDB 5wau: Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K
Enzymatic activity of Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K
All present enzymatic activity of Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K:
1.9.3.1;
Protein crystallography data
The structure of Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K, PDB code: 5wau
was solved by
R.Fromme,
I.Ishigami,
S.Y.Yeh,
N.Zatsepin,
T.Grant,
P.Fromme,
D.Rousseau,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
39.00 /
1.95
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
177.923,
182.555,
208.450,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21.7 /
24.4
|
Other elements in 5wau:
The structure of Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K
(pdb code 5wau). 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 Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K, PDB code: 5wau:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 5wau
Go back to
Copper Binding Sites List in 5wau
Copper binding site 1 out
of 6 in the Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography 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 Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:25.7
occ:1.00
|
NE2
|
A:HIS290
|
2.0
|
24.9
|
1.0
|
NE2
|
A:HIS291
|
2.1
|
24.4
|
1.0
|
ND1
|
A:HIS240
|
2.1
|
24.1
|
1.0
|
O
|
A:CMO610
|
2.2
|
46.3
|
1.0
|
C
|
A:CMO610
|
2.6
|
46.1
|
1.0
|
CE1
|
A:HIS291
|
3.0
|
22.4
|
1.0
|
CE1
|
A:HIS240
|
3.0
|
24.4
|
1.0
|
CD2
|
A:HIS290
|
3.0
|
23.7
|
1.0
|
CE1
|
A:HIS290
|
3.0
|
25.5
|
1.0
|
CD2
|
A:HIS291
|
3.0
|
22.0
|
1.0
|
CG
|
A:HIS240
|
3.1
|
22.5
|
1.0
|
CB
|
A:HIS240
|
3.5
|
21.1
|
1.0
|
ND1
|
A:HIS291
|
4.0
|
22.3
|
1.0
|
CA
|
A:HIS240
|
4.1
|
22.5
|
1.0
|
CG
|
A:HIS291
|
4.1
|
22.3
|
1.0
|
ND1
|
A:HIS290
|
4.1
|
24.5
|
1.0
|
CG
|
A:HIS290
|
4.2
|
24.6
|
1.0
|
NE2
|
A:HIS240
|
4.2
|
25.5
|
1.0
|
CD2
|
A:HIS240
|
4.2
|
24.1
|
1.0
|
C1A
|
A:HEA602
|
4.5
|
23.1
|
1.0
|
C4A
|
A:HEA602
|
4.7
|
23.0
|
1.0
|
NA
|
A:HEA602
|
4.7
|
25.4
|
1.0
|
C2A
|
A:HEA602
|
4.7
|
24.2
|
1.0
|
CG2
|
A:VAL243
|
4.8
|
23.7
|
1.0
|
C3A
|
A:HEA602
|
4.8
|
23.5
|
1.0
|
FE
|
A:HEA602
|
4.9
|
25.3
|
1.0
|
N
|
A:HIS240
|
5.0
|
21.3
|
1.0
|
|
Copper binding site 2 out
of 6 in 5wau
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Copper Binding Sites List in 5wau
Copper binding site 2 out
of 6 in the Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography 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 Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu302
b:24.6
occ:1.00
|
CU1
|
B:CUA302
|
0.0
|
24.6
|
1.0
|
ND1
|
B:HIS204
|
2.0
|
23.7
|
1.0
|
O
|
B:GLU198
|
2.1
|
30.3
|
1.0
|
SG
|
B:CYS200
|
2.2
|
24.5
|
1.0
|
SG
|
B:CYS196
|
2.3
|
24.0
|
1.0
|
CU2
|
B:CUA302
|
2.6
|
24.4
|
1.0
|
CE1
|
B:HIS204
|
2.9
|
24.9
|
1.0
|
CG
|
B:HIS204
|
3.2
|
24.4
|
1.0
|
CE
|
B:MET207
|
3.2
|
37.0
|
1.0
|
CB
|
B:CYS196
|
3.3
|
23.0
|
1.0
|
C
|
B:GLU198
|
3.3
|
28.3
|
1.0
|
CB
|
B:CYS200
|
3.4
|
24.4
|
1.0
|
CA
|
B:HIS204
|
3.6
|
23.9
|
1.0
|
CB
|
B:HIS204
|
3.7
|
24.0
|
1.0
|
N
|
B:CYS200
|
3.7
|
22.7
|
1.0
|
O
|
B:HIS204
|
3.8
|
23.1
|
1.0
|
NE2
|
B:HIS204
|
4.0
|
23.6
|
1.0
|
N
|
B:GLU198
|
4.1
|
26.7
|
1.0
|
C
|
B:HIS204
|
4.1
|
23.0
|
1.0
|
C
|
B:CYS196
|
4.2
|
23.6
|
1.0
|
N
|
B:ILE199
|
4.2
|
26.5
|
1.0
|
O
|
B:CYS196
|
4.2
|
22.3
|
1.0
|
CD2
|
B:HIS204
|
4.2
|
24.1
|
1.0
|
CA
|
B:CYS200
|
4.2
|
24.4
|
1.0
|
CA
|
B:ILE199
|
4.2
|
24.8
|
1.0
|
ND1
|
B:HIS161
|
4.3
|
23.9
|
1.0
|
C
|
B:ILE199
|
4.3
|
25.0
|
1.0
|
CA
|
B:CYS196
|
4.3
|
23.3
|
1.0
|
CA
|
B:GLU198
|
4.4
|
27.3
|
1.0
|
SD
|
B:MET207
|
4.4
|
26.9
|
1.0
|
N
|
B:SER197
|
4.6
|
25.0
|
1.0
|
N
|
B:HIS204
|
4.8
|
25.6
|
1.0
|
CG
|
B:MET207
|
4.8
|
27.6
|
1.0
|
CA
|
B:HIS161
|
4.9
|
22.8
|
1.0
|
|
Copper binding site 3 out
of 6 in 5wau
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Copper Binding Sites List in 5wau
Copper binding site 3 out
of 6 in the Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography 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 Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu302
b:24.4
occ:1.00
|
CU2
|
B:CUA302
|
0.0
|
24.4
|
1.0
|
ND1
|
B:HIS161
|
2.0
|
23.9
|
1.0
|
CE
|
B:MET207
|
2.1
|
37.0
|
1.0
|
SG
|
B:CYS196
|
2.3
|
24.0
|
1.0
|
SG
|
B:CYS200
|
2.4
|
24.5
|
1.0
|
SD
|
B:MET207
|
2.4
|
26.9
|
1.0
|
CU1
|
B:CUA302
|
2.6
|
24.6
|
1.0
|
CE1
|
B:HIS161
|
2.9
|
23.7
|
1.0
|
CG
|
B:HIS161
|
3.1
|
23.1
|
1.0
|
CB
|
B:CYS200
|
3.3
|
24.4
|
1.0
|
CB
|
B:CYS196
|
3.5
|
23.0
|
1.0
|
CG
|
B:MET207
|
3.6
|
27.6
|
1.0
|
CB
|
B:HIS161
|
3.6
|
24.2
|
1.0
|
O
|
B:GLU198
|
3.9
|
30.3
|
1.0
|
NE2
|
B:HIS161
|
4.1
|
23.1
|
1.0
|
CA
|
B:HIS161
|
4.2
|
22.8
|
1.0
|
CD2
|
B:HIS161
|
4.2
|
22.8
|
1.0
|
O
|
B:HIS102
|
4.6
|
23.9
|
1.0
|
ND1
|
B:HIS204
|
4.6
|
23.7
|
1.0
|
CD1
|
B:TRP104
|
4.6
|
26.6
|
1.0
|
O
|
B:LEU160
|
4.7
|
24.1
|
1.0
|
CA
|
B:CYS200
|
4.7
|
24.4
|
1.0
|
CA
|
B:HIS204
|
4.9
|
23.9
|
1.0
|
CA
|
B:CYS196
|
4.9
|
23.3
|
1.0
|
CB
|
B:MET207
|
5.0
|
25.9
|
1.0
|
CZ2
|
B:TRP106
|
5.0
|
26.6
|
1.0
|
|
Copper binding site 4 out
of 6 in 5wau
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Copper Binding Sites List in 5wau
Copper binding site 4 out
of 6 in the Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography 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 Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
a:Cu603
b:34.7
occ:1.00
|
ND1
|
a:HIS240
|
2.0
|
32.4
|
1.0
|
NE2
|
a:HIS290
|
2.0
|
29.7
|
1.0
|
NE2
|
a:HIS291
|
2.1
|
34.8
|
1.0
|
O
|
a:CMO608
|
2.6
|
69.0
|
1.0
|
C
|
a:CMO608
|
2.7
|
65.8
|
1.0
|
CE1
|
a:HIS291
|
2.9
|
33.8
|
1.0
|
CE1
|
a:HIS290
|
2.9
|
29.0
|
1.0
|
CE1
|
a:HIS240
|
3.0
|
33.1
|
1.0
|
CG
|
a:HIS240
|
3.0
|
33.7
|
1.0
|
CD2
|
a:HIS291
|
3.1
|
33.9
|
1.0
|
CD2
|
a:HIS290
|
3.1
|
29.7
|
1.0
|
CB
|
a:HIS240
|
3.4
|
32.5
|
1.0
|
ND1
|
a:HIS291
|
4.0
|
33.1
|
1.0
|
CG
|
a:HIS291
|
4.1
|
33.2
|
1.0
|
ND1
|
a:HIS290
|
4.1
|
29.5
|
1.0
|
CA
|
a:HIS240
|
4.1
|
32.3
|
1.0
|
NE2
|
a:HIS240
|
4.1
|
32.6
|
1.0
|
CD2
|
a:HIS240
|
4.1
|
34.4
|
1.0
|
CG
|
a:HIS290
|
4.2
|
29.4
|
1.0
|
C1A
|
a:HEA602
|
4.5
|
32.2
|
1.0
|
C4A
|
a:HEA602
|
4.7
|
31.5
|
1.0
|
C2A
|
a:HEA602
|
4.7
|
33.3
|
1.0
|
NA
|
a:HEA602
|
4.7
|
32.2
|
1.0
|
C3A
|
a:HEA602
|
4.8
|
32.4
|
1.0
|
CG2
|
a:VAL243
|
4.9
|
35.7
|
1.0
|
FE
|
a:HEA602
|
4.9
|
34.5
|
1.0
|
N
|
a:HIS240
|
5.0
|
33.2
|
1.0
|
|
Copper binding site 5 out
of 6 in 5wau
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Copper Binding Sites List in 5wau
Copper binding site 5 out
of 6 in the Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography 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 Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
b:Cu301
b:38.4
occ:1.00
|
CU1
|
b:CUA301
|
0.0
|
38.4
|
1.0
|
ND1
|
b:HIS161
|
2.0
|
44.6
|
1.0
|
SG
|
b:CYS200
|
2.3
|
35.2
|
1.0
|
SG
|
b:CYS196
|
2.3
|
37.7
|
1.0
|
SD
|
b:MET207
|
2.4
|
38.4
|
1.0
|
CU2
|
b:CUA301
|
2.7
|
37.0
|
1.0
|
CE1
|
b:HIS161
|
2.9
|
45.2
|
1.0
|
CG
|
b:HIS161
|
3.1
|
40.7
|
1.0
|
CE
|
b:MET207
|
3.1
|
40.7
|
1.0
|
CB
|
b:CYS200
|
3.3
|
37.6
|
1.0
|
CB
|
b:CYS196
|
3.5
|
42.1
|
1.0
|
CB
|
b:HIS161
|
3.5
|
38.5
|
1.0
|
CG
|
b:MET207
|
3.6
|
43.7
|
1.0
|
O
|
b:GLU198
|
3.9
|
43.0
|
1.0
|
NE2
|
b:HIS161
|
4.1
|
44.0
|
1.0
|
CA
|
b:HIS161
|
4.2
|
38.9
|
1.0
|
CD2
|
b:HIS161
|
4.2
|
41.0
|
1.0
|
O
|
b:HIS102
|
4.5
|
37.4
|
1.0
|
CD1
|
b:TRP104
|
4.6
|
42.3
|
1.0
|
ND1
|
b:HIS204
|
4.6
|
35.3
|
1.0
|
CA
|
b:CYS200
|
4.7
|
37.5
|
1.0
|
O
|
b:LEU160
|
4.8
|
34.3
|
1.0
|
CA
|
b:HIS204
|
4.9
|
38.9
|
1.0
|
CA
|
b:CYS196
|
4.9
|
40.5
|
1.0
|
CB
|
b:MET207
|
4.9
|
42.5
|
1.0
|
N
|
b:CYS200
|
4.9
|
38.5
|
1.0
|
CZ2
|
b:TRP106
|
4.9
|
42.2
|
1.0
|
|
Copper binding site 6 out
of 6 in 5wau
Go back to
Copper Binding Sites List in 5wau
Copper binding site 6 out
of 6 in the Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography 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 Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Synchrotron X-Ray Crystallography at 100 K within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
b:Cu301
b:37.0
occ:1.00
|
CU2
|
b:CUA301
|
0.0
|
37.0
|
1.0
|
ND1
|
b:HIS204
|
2.0
|
35.3
|
1.0
|
O
|
b:GLU198
|
2.1
|
43.0
|
1.0
|
SG
|
b:CYS196
|
2.3
|
37.7
|
1.0
|
SG
|
b:CYS200
|
2.3
|
35.2
|
1.0
|
CU1
|
b:CUA301
|
2.7
|
38.4
|
1.0
|
CE1
|
b:HIS204
|
2.9
|
36.1
|
1.0
|
CG
|
b:HIS204
|
3.1
|
39.1
|
1.0
|
C
|
b:GLU198
|
3.3
|
39.5
|
1.0
|
CB
|
b:CYS196
|
3.4
|
42.1
|
1.0
|
CB
|
b:CYS200
|
3.5
|
37.6
|
1.0
|
CA
|
b:HIS204
|
3.5
|
38.9
|
1.0
|
CB
|
b:HIS204
|
3.6
|
39.4
|
1.0
|
N
|
b:CYS200
|
3.6
|
38.5
|
1.0
|
O
|
b:HIS204
|
3.9
|
39.1
|
1.0
|
NE2
|
b:HIS204
|
4.0
|
35.7
|
1.0
|
O
|
b:CYS196
|
4.1
|
39.1
|
1.0
|
N
|
b:GLU198
|
4.1
|
40.6
|
1.0
|
N
|
b:ILE199
|
4.1
|
39.0
|
1.0
|
CD2
|
b:HIS204
|
4.1
|
36.8
|
1.0
|
C
|
b:CYS196
|
4.2
|
39.0
|
1.0
|
C
|
b:HIS204
|
4.2
|
38.4
|
1.0
|
CA
|
b:ILE199
|
4.2
|
39.0
|
1.0
|
CA
|
b:CYS200
|
4.2
|
37.5
|
1.0
|
C
|
b:ILE199
|
4.3
|
40.6
|
1.0
|
CA
|
b:GLU198
|
4.3
|
40.6
|
1.0
|
ND1
|
b:HIS161
|
4.4
|
44.6
|
1.0
|
CA
|
b:CYS196
|
4.4
|
40.5
|
1.0
|
SD
|
b:MET207
|
4.4
|
38.4
|
1.0
|
N
|
b:SER197
|
4.6
|
39.0
|
1.0
|
N
|
b:HIS204
|
4.7
|
41.6
|
1.0
|
CG
|
b:MET207
|
4.8
|
43.7
|
1.0
|
CA
|
b:HIS161
|
5.0
|
38.9
|
1.0
|
|
Reference:
I.Ishigami,
N.A.Zatsepin,
M.Hikita,
C.E.Conrad,
G.Nelson,
J.D.Coe,
S.Basu,
T.D.Grant,
M.H.Seaberg,
R.G.Sierra,
M.S.Hunter,
P.Fromme,
R.Fromme,
S.R.Yeh,
D.L.Rousseau.
Crystal Structure of Co-Bound Cytochrome C Oxidase Determined By Serial Femtosecond X-Ray Crystallography at Room Temperature. Proc. Natl. Acad. Sci. V. 114 8011 2017U.S.A..
ISSN: ESSN 1091-6490
PubMed: 28698372
DOI: 10.1073/PNAS.1705628114
Page generated: Wed Jul 31 05:17:33 2024
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