Copper in PDB 3omi: Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation
Enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation
All present enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation:
1.9.3.1;
Protein crystallography data
The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation, PDB code: 3omi
was solved by
J.Liu,
L.Qin,
S.Ferguson-Miller,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
35.84 /
2.15
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
125.064,
131.519,
175.674,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.2 /
21.5
|
Other elements in 3omi:
The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation
(pdb code 3omi). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation, PDB code: 3omi:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 3omi
Go back to
Copper Binding Sites List in 3omi
Copper binding site 1 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu611
b:28.2
occ:1.00
|
NE2
|
A:HIS333
|
2.0
|
30.0
|
1.0
|
NE2
|
A:HIS334
|
2.1
|
28.2
|
1.0
|
ND1
|
A:HIS284
|
2.2
|
25.5
|
1.0
|
O
|
A:OH601
|
2.4
|
17.9
|
1.0
|
O
|
A:HOH744
|
2.8
|
18.4
|
1.0
|
CE1
|
A:HIS333
|
2.9
|
31.5
|
1.0
|
CE1
|
A:HIS334
|
2.9
|
26.0
|
1.0
|
CD2
|
A:HIS334
|
3.1
|
26.1
|
1.0
|
CD2
|
A:HIS333
|
3.1
|
28.1
|
1.0
|
CG
|
A:HIS284
|
3.2
|
25.1
|
1.0
|
CE1
|
A:HIS284
|
3.2
|
25.5
|
1.0
|
CB
|
A:HIS284
|
3.4
|
24.6
|
1.0
|
CA
|
A:HIS284
|
4.0
|
24.6
|
1.0
|
ND1
|
A:HIS334
|
4.0
|
25.9
|
1.0
|
ND1
|
A:HIS333
|
4.1
|
29.3
|
1.0
|
CG
|
A:HIS334
|
4.1
|
26.2
|
1.0
|
CG
|
A:HIS333
|
4.2
|
27.9
|
1.0
|
CD2
|
A:HIS284
|
4.3
|
26.4
|
1.0
|
NE2
|
A:HIS284
|
4.3
|
25.9
|
1.0
|
NA
|
A:HEA608
|
4.4
|
24.4
|
1.0
|
C1A
|
A:HEA608
|
4.5
|
24.2
|
1.0
|
C4A
|
A:HEA608
|
4.5
|
24.3
|
1.0
|
N
|
A:HIS284
|
4.8
|
24.4
|
1.0
|
FE
|
A:HEA608
|
4.8
|
24.3
|
1.0
|
C2A
|
A:HEA608
|
4.8
|
24.7
|
1.0
|
C3A
|
A:HEA608
|
4.8
|
26.1
|
1.0
|
CHA
|
A:HEA608
|
5.0
|
21.8
|
1.0
|
|
Copper binding site 2 out
of 6 in 3omi
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Copper Binding Sites List in 3omi
Copper binding site 2 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu307
b:21.7
occ:1.00
|
ND1
|
B:HIS260
|
2.1
|
16.7
|
1.0
|
SG
|
B:CYS252
|
2.3
|
20.5
|
1.0
|
SG
|
B:CYS256
|
2.3
|
19.9
|
1.0
|
O
|
B:GLU254
|
2.6
|
21.4
|
1.0
|
CU
|
B:CU1308
|
2.6
|
21.0
|
1.0
|
CE1
|
B:HIS260
|
3.0
|
17.0
|
1.0
|
CG
|
B:HIS260
|
3.1
|
18.1
|
1.0
|
CB
|
B:CYS252
|
3.3
|
19.8
|
1.0
|
CB
|
B:CYS256
|
3.5
|
20.5
|
1.0
|
C
|
B:GLU254
|
3.5
|
21.6
|
1.0
|
CB
|
B:HIS260
|
3.5
|
16.9
|
1.0
|
CA
|
B:HIS260
|
3.6
|
18.4
|
1.0
|
N
|
B:CYS256
|
3.7
|
20.4
|
1.0
|
O
|
B:HIS260
|
3.9
|
18.2
|
1.0
|
N
|
B:GLU254
|
4.1
|
22.5
|
1.0
|
NE2
|
B:HIS260
|
4.1
|
18.8
|
1.0
|
C
|
B:CYS252
|
4.2
|
20.8
|
1.0
|
C
|
B:HIS260
|
4.2
|
18.3
|
1.0
|
CA
|
B:LEU255
|
4.2
|
20.7
|
1.0
|
O
|
B:CYS252
|
4.2
|
19.6
|
1.0
|
CD2
|
B:HIS260
|
4.2
|
16.5
|
1.0
|
C
|
B:LEU255
|
4.2
|
20.6
|
1.0
|
CA
|
B:CYS256
|
4.2
|
20.2
|
1.0
|
N
|
B:LEU255
|
4.2
|
20.8
|
1.0
|
ND1
|
B:HIS217
|
4.3
|
18.4
|
1.0
|
CA
|
B:CYS252
|
4.3
|
20.1
|
1.0
|
SD
|
B:MET263
|
4.5
|
19.0
|
1.0
|
CA
|
B:GLU254
|
4.5
|
22.3
|
1.0
|
N
|
B:SER253
|
4.6
|
21.7
|
1.0
|
CG
|
B:MET263
|
4.7
|
18.0
|
1.0
|
N
|
B:HIS260
|
4.8
|
18.4
|
1.0
|
CA
|
B:HIS217
|
4.9
|
19.6
|
1.0
|
|
Copper binding site 3 out
of 6 in 3omi
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Copper Binding Sites List in 3omi
Copper binding site 3 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu308
b:21.0
occ:1.00
|
ND1
|
B:HIS217
|
2.1
|
18.4
|
1.0
|
SG
|
B:CYS252
|
2.3
|
20.5
|
1.0
|
SG
|
B:CYS256
|
2.4
|
19.9
|
1.0
|
SD
|
B:MET263
|
2.4
|
19.0
|
1.0
|
CU
|
B:CU307
|
2.6
|
21.7
|
1.0
|
CE1
|
B:HIS217
|
3.0
|
19.8
|
1.0
|
CE
|
B:MET263
|
3.0
|
16.5
|
1.0
|
CG
|
B:HIS217
|
3.2
|
19.8
|
1.0
|
CB
|
B:CYS256
|
3.4
|
20.5
|
1.0
|
CB
|
B:CYS252
|
3.5
|
19.8
|
1.0
|
CG
|
B:MET263
|
3.5
|
18.0
|
1.0
|
CB
|
B:HIS217
|
3.6
|
18.9
|
1.0
|
NE2
|
B:HIS217
|
4.1
|
19.4
|
1.0
|
CA
|
B:HIS217
|
4.2
|
19.6
|
1.0
|
O
|
B:GLU254
|
4.3
|
21.4
|
1.0
|
CD2
|
B:HIS217
|
4.3
|
19.9
|
1.0
|
CD1
|
B:TRP143
|
4.4
|
21.0
|
1.0
|
ND1
|
B:HIS260
|
4.6
|
16.7
|
1.0
|
O
|
B:TYR141
|
4.7
|
21.7
|
1.0
|
CA
|
B:HIS260
|
4.7
|
18.4
|
1.0
|
CA
|
B:CYS256
|
4.8
|
20.2
|
1.0
|
CA
|
B:CYS252
|
4.8
|
20.1
|
1.0
|
CB
|
B:MET263
|
4.9
|
19.2
|
1.0
|
|
Copper binding site 4 out
of 6 in 3omi
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Copper Binding Sites List in 3omi
Copper binding site 4 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu608
b:35.5
occ:1.00
|
NE2
|
C:HIS333
|
2.1
|
32.1
|
1.0
|
NE2
|
C:HIS334
|
2.1
|
34.6
|
1.0
|
ND1
|
C:HIS284
|
2.2
|
35.2
|
1.0
|
O
|
C:OH601
|
2.3
|
27.1
|
1.0
|
O
|
C:HOH795
|
2.8
|
25.4
|
1.0
|
CE1
|
C:HIS333
|
3.0
|
31.8
|
1.0
|
CD2
|
C:HIS334
|
3.0
|
30.9
|
1.0
|
CE1
|
C:HIS334
|
3.0
|
31.7
|
1.0
|
CE1
|
C:HIS284
|
3.1
|
35.9
|
1.0
|
CG
|
C:HIS284
|
3.2
|
36.2
|
1.0
|
CD2
|
C:HIS333
|
3.2
|
31.8
|
1.0
|
CB
|
C:HIS284
|
3.4
|
35.0
|
1.0
|
CA
|
C:HIS284
|
4.0
|
35.1
|
1.0
|
ND1
|
C:HIS334
|
4.1
|
31.4
|
1.0
|
CG
|
C:HIS334
|
4.1
|
31.2
|
1.0
|
ND1
|
C:HIS333
|
4.1
|
31.6
|
1.0
|
CD2
|
C:HIS284
|
4.3
|
36.8
|
1.0
|
CG
|
C:HIS333
|
4.3
|
32.1
|
1.0
|
NE2
|
C:HIS284
|
4.3
|
36.4
|
1.0
|
NA
|
C:HEA606
|
4.5
|
30.5
|
1.0
|
C1A
|
C:HEA606
|
4.5
|
29.8
|
1.0
|
C4A
|
C:HEA606
|
4.6
|
32.1
|
1.0
|
FE
|
C:HEA606
|
4.8
|
29.0
|
1.0
|
C2A
|
C:HEA606
|
4.8
|
30.5
|
1.0
|
N
|
C:HIS284
|
4.8
|
35.0
|
1.0
|
C3A
|
C:HEA606
|
4.8
|
30.3
|
1.0
|
CG2
|
C:VAL287
|
5.0
|
34.0
|
1.0
|
CHA
|
C:HEA606
|
5.0
|
29.9
|
1.0
|
|
Copper binding site 5 out
of 6 in 3omi
Go back to
Copper Binding Sites List in 3omi
Copper binding site 5 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu305
b:27.3
occ:1.00
|
ND1
|
D:HIS260
|
2.1
|
27.0
|
1.0
|
SG
|
D:CYS252
|
2.3
|
24.1
|
1.0
|
SG
|
D:CYS256
|
2.3
|
25.7
|
1.0
|
CU
|
D:CU1306
|
2.6
|
26.9
|
1.0
|
O
|
D:GLU254
|
2.6
|
27.7
|
1.0
|
CE1
|
D:HIS260
|
2.9
|
26.3
|
1.0
|
CG
|
D:HIS260
|
3.2
|
26.5
|
1.0
|
CB
|
D:CYS252
|
3.2
|
23.8
|
1.0
|
CB
|
D:CYS256
|
3.4
|
27.3
|
1.0
|
C
|
D:GLU254
|
3.6
|
27.7
|
1.0
|
CA
|
D:HIS260
|
3.6
|
26.7
|
1.0
|
CB
|
D:HIS260
|
3.6
|
26.7
|
1.0
|
N
|
D:CYS256
|
3.7
|
27.4
|
1.0
|
O
|
D:HIS260
|
3.9
|
26.1
|
1.0
|
NE2
|
D:HIS260
|
4.0
|
26.5
|
1.0
|
N
|
D:GLU254
|
4.1
|
27.4
|
1.0
|
C
|
D:CYS252
|
4.1
|
25.0
|
1.0
|
CA
|
D:CYS256
|
4.2
|
27.1
|
1.0
|
CD2
|
D:HIS260
|
4.2
|
26.4
|
1.0
|
ND1
|
D:HIS217
|
4.2
|
25.5
|
1.0
|
C
|
D:HIS260
|
4.2
|
26.6
|
1.0
|
O
|
D:CYS252
|
4.3
|
24.2
|
1.0
|
CA
|
D:LEU255
|
4.3
|
27.8
|
1.0
|
C
|
D:LEU255
|
4.3
|
27.5
|
1.0
|
CA
|
D:CYS252
|
4.3
|
24.5
|
1.0
|
N
|
D:LEU255
|
4.3
|
27.6
|
1.0
|
SD
|
D:MET263
|
4.4
|
27.2
|
1.0
|
CA
|
D:GLU254
|
4.5
|
27.9
|
1.0
|
N
|
D:SER253
|
4.5
|
25.8
|
1.0
|
CG
|
D:MET263
|
4.6
|
26.3
|
1.0
|
N
|
D:HIS260
|
4.8
|
27.6
|
1.0
|
CA
|
D:HIS217
|
4.9
|
26.8
|
1.0
|
CB
|
D:HIS217
|
5.0
|
27.1
|
1.0
|
|
Copper binding site 6 out
of 6 in 3omi
Go back to
Copper Binding Sites List in 3omi
Copper binding site 6 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu306
b:26.9
occ:1.00
|
ND1
|
D:HIS217
|
2.1
|
25.5
|
1.0
|
SG
|
D:CYS252
|
2.3
|
24.1
|
1.0
|
SG
|
D:CYS256
|
2.4
|
25.7
|
1.0
|
SD
|
D:MET263
|
2.4
|
27.2
|
1.0
|
CU
|
D:CU305
|
2.6
|
27.3
|
1.0
|
CE1
|
D:HIS217
|
3.0
|
25.7
|
1.0
|
CE
|
D:MET263
|
3.0
|
26.8
|
1.0
|
CG
|
D:HIS217
|
3.1
|
25.5
|
1.0
|
CB
|
D:CYS256
|
3.3
|
27.3
|
1.0
|
CG
|
D:MET263
|
3.4
|
26.3
|
1.0
|
CB
|
D:CYS252
|
3.4
|
23.8
|
1.0
|
CB
|
D:HIS217
|
3.5
|
27.1
|
1.0
|
NE2
|
D:HIS217
|
4.1
|
24.3
|
1.0
|
CA
|
D:HIS217
|
4.2
|
26.8
|
1.0
|
CD2
|
D:HIS217
|
4.2
|
23.9
|
1.0
|
O
|
D:GLU254
|
4.3
|
27.7
|
1.0
|
CD1
|
D:TRP143
|
4.4
|
31.4
|
1.0
|
ND1
|
D:HIS260
|
4.5
|
27.0
|
1.0
|
CA
|
D:CYS256
|
4.7
|
27.1
|
1.0
|
O
|
D:TYR141
|
4.7
|
29.1
|
1.0
|
CA
|
D:HIS260
|
4.8
|
26.7
|
1.0
|
CB
|
D:MET263
|
4.8
|
27.4
|
1.0
|
CA
|
D:CYS252
|
4.8
|
24.5
|
1.0
|
CZ2
|
D:TRP145
|
5.0
|
29.0
|
1.0
|
|
Reference:
J.Liu,
L.Qin,
S.Ferguson-Miller.
Crystallographic and Online Spectral Evidence For Role of Conformational Change and Conserved Water in Cytochrome Oxidase Proton Pump. Proc.Natl.Acad.Sci.Usa V. 108 1284 2011.
ISSN: ISSN 0027-8424
PubMed: 21205904
DOI: 10.1073/PNAS.1012846108
Page generated: Wed Jul 31 01:28:45 2024
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