Copper in PDB 7y44: Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution
Enzymatic activity of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution
All present enzymatic activity of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution:
7.1.1.9;
Protein crystallography data
The structure of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution, PDB code: 7y44
was solved by
T.Tsukihara,
K.Hirata,
H.Ago,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
27.31 /
1.90
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
182.6,
204.51,
178.29,
90,
90,
90
|
R / Rfree (%)
|
18.5 /
22.7
|
Other elements in 7y44:
The structure of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution
(pdb code 7y44). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution, PDB code: 7y44:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 7y44
Go back to
Copper Binding Sites List in 7y44
Copper binding site 1 out
of 6 in the Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu603
b:17.1
occ:1.00
|
NE2
|
A:HIS291
|
2.0
|
16.4
|
1.0
|
NE2
|
A:HIS290
|
2.0
|
15.8
|
1.0
|
ND1
|
A:HIS240
|
2.0
|
17.1
|
1.0
|
O2
|
A:PER606
|
2.1
|
15.8
|
1.0
|
O1
|
A:PER606
|
2.7
|
12.6
|
1.0
|
CE1
|
A:HIS290
|
2.9
|
18.9
|
1.0
|
CE1
|
A:HIS291
|
2.9
|
17.1
|
1.0
|
CD2
|
A:HIS291
|
3.0
|
14.7
|
1.0
|
CE1
|
A:HIS240
|
3.0
|
17.2
|
1.0
|
CG
|
A:HIS240
|
3.0
|
18.3
|
1.0
|
CD2
|
A:HIS290
|
3.1
|
18.8
|
1.0
|
CB
|
A:HIS240
|
3.4
|
12.7
|
1.0
|
CA
|
A:HIS240
|
3.9
|
13.2
|
1.0
|
ND1
|
A:HIS291
|
4.1
|
15.8
|
1.0
|
ND1
|
A:HIS290
|
4.1
|
19.9
|
1.0
|
CG
|
A:HIS291
|
4.1
|
17.0
|
1.0
|
NE2
|
A:HIS240
|
4.1
|
17.9
|
1.0
|
CD2
|
A:HIS240
|
4.1
|
16.6
|
1.0
|
CG
|
A:HIS290
|
4.2
|
17.4
|
1.0
|
NA
|
A:HEA602
|
4.5
|
15.6
|
1.0
|
C1A
|
A:HEA602
|
4.5
|
17.5
|
1.0
|
C4A
|
A:HEA602
|
4.7
|
18.7
|
1.0
|
N
|
A:HIS240
|
4.7
|
14.8
|
1.0
|
C2A
|
A:HEA602
|
4.8
|
23.6
|
1.0
|
C3A
|
A:HEA602
|
4.9
|
21.2
|
1.0
|
CG2
|
A:VAL243
|
4.9
|
15.9
|
1.0
|
FE
|
A:HEA602
|
4.9
|
17.1
|
1.0
|
CHA
|
A:HEA602
|
4.9
|
13.8
|
1.0
|
|
Copper binding site 2 out
of 6 in 7y44
Go back to
Copper Binding Sites List in 7y44
Copper binding site 2 out
of 6 in the Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu302
b:19.3
occ:1.00
|
CU1
|
B:CUA302
|
0.0
|
19.3
|
1.0
|
ND1
|
B:HIS161
|
2.0
|
18.1
|
1.0
|
SG
|
B:CYS196
|
2.3
|
19.1
|
1.0
|
SG
|
B:CYS200
|
2.3
|
18.3
|
1.0
|
SD
|
B:MET207
|
2.4
|
20.6
|
1.0
|
CU2
|
B:CUA302
|
2.5
|
18.9
|
1.0
|
CE1
|
B:HIS161
|
2.9
|
17.9
|
1.0
|
CE
|
B:MET207
|
3.1
|
24.6
|
1.0
|
CG
|
B:HIS161
|
3.2
|
18.1
|
1.0
|
CB
|
B:CYS200
|
3.4
|
16.4
|
1.0
|
CB
|
B:CYS196
|
3.4
|
20.0
|
1.0
|
CG
|
B:MET207
|
3.4
|
16.8
|
1.0
|
CB
|
B:HIS161
|
3.7
|
16.5
|
1.0
|
NE2
|
B:HIS161
|
4.0
|
16.1
|
1.0
|
O
|
B:GLU198
|
4.2
|
19.5
|
1.0
|
CD2
|
B:HIS161
|
4.2
|
17.9
|
1.0
|
CA
|
B:HIS161
|
4.3
|
21.8
|
1.0
|
ND1
|
B:HIS204
|
4.4
|
17.5
|
1.0
|
O
|
B:LEU160
|
4.7
|
16.6
|
1.0
|
CA
|
B:HIS204
|
4.7
|
21.3
|
1.0
|
O
|
B:HIS102
|
4.7
|
20.9
|
1.0
|
CA
|
B:CYS196
|
4.7
|
19.7
|
1.0
|
CD1
|
B:TRP104
|
4.7
|
17.6
|
1.0
|
CA
|
B:CYS200
|
4.8
|
19.1
|
1.0
|
CB
|
B:MET207
|
4.8
|
18.7
|
1.0
|
O
|
B:HIS204
|
4.9
|
18.1
|
1.0
|
|
Copper binding site 3 out
of 6 in 7y44
Go back to
Copper Binding Sites List in 7y44
Copper binding site 3 out
of 6 in the Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu302
b:18.9
occ:1.00
|
CU2
|
B:CUA302
|
0.0
|
18.9
|
1.0
|
ND1
|
B:HIS204
|
2.0
|
17.5
|
1.0
|
SG
|
B:CYS200
|
2.2
|
18.3
|
1.0
|
SG
|
B:CYS196
|
2.3
|
19.1
|
1.0
|
CU1
|
B:CUA302
|
2.5
|
19.3
|
1.0
|
O
|
B:GLU198
|
2.5
|
19.5
|
1.0
|
CE1
|
B:HIS204
|
2.9
|
18.2
|
1.0
|
CG
|
B:HIS204
|
3.1
|
16.9
|
1.0
|
CB
|
B:CYS196
|
3.3
|
20.0
|
1.0
|
CB
|
B:CYS200
|
3.4
|
16.4
|
1.0
|
CB
|
B:HIS204
|
3.5
|
18.6
|
1.0
|
C
|
B:GLU198
|
3.6
|
19.8
|
1.0
|
CA
|
B:HIS204
|
3.6
|
21.3
|
1.0
|
N
|
B:CYS200
|
3.7
|
20.7
|
1.0
|
O
|
B:HIS204
|
3.8
|
18.1
|
1.0
|
NE2
|
B:HIS204
|
4.0
|
21.2
|
1.0
|
C
|
B:HIS204
|
4.1
|
17.2
|
1.0
|
ND1
|
B:HIS161
|
4.1
|
18.1
|
1.0
|
C
|
B:ILE199
|
4.1
|
13.7
|
1.0
|
CA
|
B:CYS200
|
4.1
|
19.1
|
1.0
|
CD2
|
B:HIS204
|
4.2
|
17.8
|
1.0
|
N
|
B:GLU198
|
4.2
|
19.1
|
1.0
|
O
|
B:CYS196
|
4.2
|
16.7
|
1.0
|
C
|
B:CYS196
|
4.3
|
21.7
|
1.0
|
CA
|
B:ILE199
|
4.3
|
23.2
|
1.0
|
SD
|
B:MET207
|
4.3
|
20.6
|
1.0
|
N
|
B:ILE199
|
4.4
|
17.2
|
1.0
|
CA
|
B:CYS196
|
4.4
|
19.7
|
1.0
|
CG
|
B:MET207
|
4.5
|
16.8
|
1.0
|
CA
|
B:GLU198
|
4.5
|
18.9
|
1.0
|
N
|
B:SER197
|
4.7
|
16.4
|
1.0
|
N
|
B:HIS204
|
4.8
|
21.3
|
1.0
|
CE1
|
B:HIS161
|
4.9
|
17.9
|
1.0
|
O
|
B:ILE199
|
5.0
|
19.6
|
1.0
|
|
Copper binding site 4 out
of 6 in 7y44
Go back to
Copper Binding Sites List in 7y44
Copper binding site 4 out
of 6 in the Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
N:Cu603
b:18.6
occ:1.00
|
NE2
|
N:HIS291
|
2.0
|
19.1
|
1.0
|
NE2
|
N:HIS290
|
2.0
|
20.7
|
1.0
|
ND1
|
N:HIS240
|
2.1
|
14.6
|
1.0
|
O2
|
N:PER606
|
2.1
|
17.8
|
1.0
|
O1
|
N:PER606
|
2.7
|
18.1
|
1.0
|
CE1
|
N:HIS291
|
2.9
|
12.0
|
1.0
|
CD2
|
N:HIS291
|
3.0
|
15.6
|
1.0
|
CG
|
N:HIS240
|
3.0
|
17.0
|
1.0
|
CD2
|
N:HIS290
|
3.0
|
19.6
|
1.0
|
CE1
|
N:HIS290
|
3.1
|
24.3
|
1.0
|
CE1
|
N:HIS240
|
3.1
|
22.5
|
1.0
|
CB
|
N:HIS240
|
3.3
|
17.4
|
1.0
|
CA
|
N:HIS240
|
3.9
|
18.3
|
1.0
|
ND1
|
N:HIS291
|
4.0
|
18.3
|
1.0
|
CG
|
N:HIS291
|
4.1
|
13.1
|
1.0
|
ND1
|
N:HIS290
|
4.2
|
17.5
|
1.0
|
CD2
|
N:HIS240
|
4.2
|
17.9
|
1.0
|
CG
|
N:HIS290
|
4.2
|
23.6
|
1.0
|
NE2
|
N:HIS240
|
4.2
|
23.8
|
1.0
|
NA
|
N:HEA602
|
4.5
|
18.2
|
1.0
|
C1A
|
N:HEA602
|
4.5
|
20.8
|
1.0
|
C4A
|
N:HEA602
|
4.7
|
24.6
|
1.0
|
N
|
N:HIS240
|
4.7
|
18.1
|
1.0
|
C2A
|
N:HEA602
|
4.8
|
17.8
|
1.0
|
C3A
|
N:HEA602
|
4.9
|
17.9
|
1.0
|
FE
|
N:HEA602
|
4.9
|
17.6
|
1.0
|
CG2
|
N:VAL243
|
5.0
|
13.2
|
1.0
|
CHA
|
N:HEA602
|
5.0
|
17.0
|
1.0
|
|
Copper binding site 5 out
of 6 in 7y44
Go back to
Copper Binding Sites List in 7y44
Copper binding site 5 out
of 6 in the Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu302
b:22.8
occ:1.00
|
CU1
|
O:CUA302
|
0.0
|
22.8
|
1.0
|
ND1
|
O:HIS161
|
2.0
|
21.4
|
1.0
|
SG
|
O:CYS200
|
2.3
|
21.5
|
1.0
|
SG
|
O:CYS196
|
2.3
|
23.8
|
1.0
|
SD
|
O:MET207
|
2.5
|
27.1
|
1.0
|
CU2
|
O:CUA302
|
2.5
|
22.8
|
1.0
|
CE1
|
O:HIS161
|
2.8
|
22.8
|
1.0
|
CG
|
O:HIS161
|
3.2
|
23.2
|
1.0
|
CE
|
O:MET207
|
3.2
|
22.2
|
1.0
|
CB
|
O:CYS200
|
3.3
|
20.9
|
1.0
|
CB
|
O:CYS196
|
3.4
|
20.4
|
1.0
|
CG
|
O:MET207
|
3.6
|
24.8
|
1.0
|
CB
|
O:HIS161
|
3.7
|
27.5
|
1.0
|
NE2
|
O:HIS161
|
4.0
|
24.3
|
1.0
|
O
|
O:GLU198
|
4.1
|
21.1
|
1.0
|
CA
|
O:HIS161
|
4.2
|
24.8
|
1.0
|
CD2
|
O:HIS161
|
4.2
|
19.9
|
1.0
|
ND1
|
O:HIS204
|
4.5
|
24.3
|
1.0
|
CA
|
O:CYS200
|
4.7
|
22.7
|
1.0
|
O
|
O:LEU160
|
4.7
|
27.7
|
1.0
|
CA
|
O:HIS204
|
4.7
|
26.4
|
1.0
|
O
|
O:HIS102
|
4.8
|
26.9
|
1.0
|
CA
|
O:CYS196
|
4.8
|
24.6
|
1.0
|
CD1
|
O:TRP104
|
4.8
|
20.4
|
1.0
|
O
|
O:HIS204
|
4.9
|
24.5
|
1.0
|
|
Copper binding site 6 out
of 6 in 7y44
Go back to
Copper Binding Sites List in 7y44
Copper binding site 6 out
of 6 in the Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Re-Refinement of Damage Free X-Ray Structure of Bovine Cytochrome C Oxidase at 1.9 Angstrom Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
O:Cu302
b:22.8
occ:1.00
|
CU2
|
O:CUA302
|
0.0
|
22.8
|
1.0
|
ND1
|
O:HIS204
|
2.0
|
24.3
|
1.0
|
SG
|
O:CYS200
|
2.3
|
21.5
|
1.0
|
SG
|
O:CYS196
|
2.3
|
23.8
|
1.0
|
CU1
|
O:CUA302
|
2.5
|
22.8
|
1.0
|
O
|
O:GLU198
|
2.5
|
21.1
|
1.0
|
CE1
|
O:HIS204
|
2.9
|
23.4
|
1.0
|
CG
|
O:HIS204
|
3.1
|
21.3
|
1.0
|
CB
|
O:CYS200
|
3.3
|
20.9
|
1.0
|
CB
|
O:CYS196
|
3.4
|
20.4
|
1.0
|
CB
|
O:HIS204
|
3.5
|
29.1
|
1.0
|
C
|
O:GLU198
|
3.5
|
22.3
|
1.0
|
CA
|
O:HIS204
|
3.6
|
26.4
|
1.0
|
N
|
O:CYS200
|
3.7
|
25.1
|
1.0
|
O
|
O:HIS204
|
3.8
|
24.5
|
1.0
|
NE2
|
O:HIS204
|
4.1
|
19.7
|
1.0
|
CA
|
O:CYS200
|
4.1
|
22.7
|
1.0
|
C
|
O:HIS204
|
4.1
|
27.2
|
1.0
|
C
|
O:ILE199
|
4.1
|
28.0
|
1.0
|
CD2
|
O:HIS204
|
4.2
|
23.4
|
1.0
|
ND1
|
O:HIS161
|
4.2
|
21.4
|
1.0
|
N
|
O:GLU198
|
4.2
|
19.5
|
1.0
|
CA
|
O:ILE199
|
4.3
|
20.6
|
1.0
|
C
|
O:CYS196
|
4.3
|
28.1
|
1.0
|
O
|
O:CYS196
|
4.3
|
21.2
|
1.0
|
N
|
O:ILE199
|
4.3
|
20.4
|
1.0
|
SD
|
O:MET207
|
4.4
|
27.1
|
1.0
|
CA
|
O:CYS196
|
4.5
|
24.6
|
1.0
|
CA
|
O:GLU198
|
4.5
|
20.6
|
1.0
|
N
|
O:SER197
|
4.7
|
21.1
|
1.0
|
CG
|
O:MET207
|
4.7
|
24.8
|
1.0
|
N
|
O:HIS204
|
4.8
|
23.8
|
1.0
|
CE1
|
O:HIS161
|
4.9
|
22.8
|
1.0
|
O
|
O:ILE199
|
4.9
|
23.1
|
1.0
|
C
|
O:CYS200
|
5.0
|
31.9
|
1.0
|
CA
|
O:HIS161
|
5.0
|
24.8
|
1.0
|
|
Reference:
K.Hirata,
T.Tsukihara,
H.Ago.
Determination of Damage-Free Crystal Structure of An X-Ray-Sensitive Protein Using An Xfel Nature Methods V. 11 734 2014.
DOI: 10.1038/NMETH.2962
Page generated: Wed Jul 31 09:23:37 2024
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