Copper in PDB 3omn: Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation in the Reduced State
Enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation in the Reduced State
All present enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation in the Reduced State:
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 in the Reduced State, PDB code: 3omn
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)
|
42.70 /
2.15
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
124.670,
132.033,
176.286,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.8 /
21.9
|
Other elements in 3omn:
The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with D132A Mutation in the Reduced State 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 in the Reduced State
(pdb code 3omn). 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 in the Reduced State, PDB code: 3omn:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 3omn
Go back to
Copper Binding Sites List in 3omn
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 in the Reduced State
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 in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu5
b:37.3
occ:1.00
|
NE2
|
A:HIS334
|
2.0
|
34.6
|
1.0
|
ND1
|
A:HIS284
|
2.2
|
32.5
|
1.0
|
NE2
|
A:HIS333
|
2.3
|
37.6
|
1.0
|
O
|
A:OH802
|
2.6
|
8.4
|
0.4
|
O
|
A:HOH701
|
2.6
|
31.0
|
0.6
|
O
|
A:HOH701
|
2.8
|
12.9
|
0.4
|
CD2
|
A:HIS334
|
3.0
|
32.3
|
1.0
|
CE1
|
A:HIS334
|
3.0
|
31.8
|
1.0
|
CE1
|
A:HIS333
|
3.1
|
38.4
|
1.0
|
CE1
|
A:HIS284
|
3.1
|
32.3
|
1.0
|
CG
|
A:HIS284
|
3.2
|
31.8
|
1.0
|
CD2
|
A:HIS333
|
3.3
|
35.3
|
1.0
|
CB
|
A:HIS284
|
3.5
|
30.6
|
1.0
|
CA
|
A:HIS284
|
4.0
|
30.9
|
1.0
|
ND1
|
A:HIS334
|
4.0
|
31.4
|
1.0
|
CG
|
A:HIS334
|
4.1
|
31.8
|
1.0
|
NE2
|
A:HIS284
|
4.2
|
32.4
|
1.0
|
ND1
|
A:HIS333
|
4.2
|
37.2
|
1.0
|
CD2
|
A:HIS284
|
4.3
|
32.4
|
1.0
|
CG
|
A:HIS333
|
4.4
|
34.7
|
1.0
|
NA
|
A:HEA2
|
4.5
|
21.3
|
0.4
|
C1A
|
A:HEA2
|
4.7
|
21.8
|
0.4
|
C4A
|
A:HEA2
|
4.7
|
22.4
|
0.4
|
ND
|
A:HEA2
|
4.7
|
33.9
|
0.6
|
N
|
A:HIS284
|
4.7
|
31.0
|
1.0
|
FE
|
A:HEA2
|
4.8
|
22.1
|
0.4
|
C1A
|
A:HEA2
|
4.8
|
33.6
|
0.6
|
C4D
|
A:HEA2
|
4.9
|
33.5
|
0.6
|
NA
|
A:HEA2
|
4.9
|
33.2
|
0.6
|
CG2
|
A:VAL330
|
5.0
|
35.3
|
1.0
|
CG2
|
A:VAL287
|
5.0
|
30.9
|
1.0
|
C3A
|
A:HEA2
|
5.0
|
22.8
|
0.4
|
C2A
|
A:HEA2
|
5.0
|
22.4
|
0.4
|
|
Copper binding site 2 out
of 6 in 3omn
Go back to
Copper Binding Sites List in 3omn
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 in the Reduced State
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 in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu287
b:25.6
occ:1.00
|
ND1
|
B:HIS260
|
2.1
|
25.0
|
1.0
|
SG
|
B:CYS252
|
2.2
|
24.6
|
1.0
|
SG
|
B:CYS256
|
2.3
|
25.4
|
1.0
|
CU
|
B:CU1288
|
2.6
|
26.0
|
1.0
|
O
|
B:GLU254
|
2.6
|
24.5
|
1.0
|
CE1
|
B:HIS260
|
2.9
|
24.7
|
1.0
|
CG
|
B:HIS260
|
3.2
|
25.2
|
1.0
|
CB
|
B:CYS252
|
3.3
|
24.6
|
1.0
|
CB
|
B:CYS256
|
3.5
|
25.9
|
1.0
|
C
|
B:GLU254
|
3.6
|
24.9
|
1.0
|
CA
|
B:HIS260
|
3.6
|
24.5
|
1.0
|
CB
|
B:HIS260
|
3.6
|
24.2
|
1.0
|
N
|
B:CYS256
|
3.7
|
25.5
|
1.0
|
O
|
B:HIS260
|
3.9
|
24.3
|
1.0
|
NE2
|
B:HIS260
|
4.1
|
25.2
|
1.0
|
N
|
B:GLU254
|
4.1
|
25.6
|
1.0
|
C
|
B:CYS252
|
4.1
|
25.2
|
1.0
|
O
|
B:CYS252
|
4.1
|
25.0
|
1.0
|
CA
|
B:LEU255
|
4.2
|
24.8
|
1.0
|
CD2
|
B:HIS260
|
4.2
|
23.5
|
1.0
|
C
|
B:HIS260
|
4.2
|
24.3
|
1.0
|
CA
|
B:CYS256
|
4.2
|
25.8
|
1.0
|
C
|
B:LEU255
|
4.2
|
25.1
|
1.0
|
N
|
B:LEU255
|
4.3
|
24.9
|
1.0
|
ND1
|
B:HIS217
|
4.3
|
24.6
|
1.0
|
CA
|
B:CYS252
|
4.4
|
24.9
|
1.0
|
CA
|
B:GLU254
|
4.5
|
25.6
|
1.0
|
SD
|
B:MET263
|
4.5
|
23.2
|
1.0
|
N
|
B:SER253
|
4.6
|
25.2
|
1.0
|
CG
|
B:MET263
|
4.8
|
23.0
|
1.0
|
N
|
B:HIS260
|
4.8
|
25.1
|
1.0
|
CA
|
B:HIS217
|
4.9
|
25.6
|
1.0
|
|
Copper binding site 3 out
of 6 in 3omn
Go back to
Copper Binding Sites List in 3omn
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 in the Reduced State
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 in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu288
b:26.0
occ:1.00
|
ND1
|
B:HIS217
|
2.1
|
24.6
|
1.0
|
SG
|
B:CYS252
|
2.3
|
24.6
|
1.0
|
SG
|
B:CYS256
|
2.4
|
25.4
|
1.0
|
SD
|
B:MET263
|
2.4
|
23.2
|
1.0
|
CU
|
B:CU1287
|
2.6
|
25.6
|
1.0
|
CE
|
B:MET263
|
2.9
|
17.6
|
1.0
|
CE1
|
B:HIS217
|
3.0
|
23.6
|
1.0
|
CG
|
B:HIS217
|
3.2
|
23.7
|
1.0
|
CB
|
B:CYS256
|
3.4
|
25.9
|
1.0
|
CB
|
B:CYS252
|
3.5
|
24.6
|
1.0
|
CG
|
B:MET263
|
3.5
|
23.0
|
1.0
|
CB
|
B:HIS217
|
3.6
|
24.8
|
1.0
|
NE2
|
B:HIS217
|
4.1
|
25.2
|
1.0
|
CA
|
B:HIS217
|
4.2
|
25.6
|
1.0
|
CD2
|
B:HIS217
|
4.3
|
23.4
|
1.0
|
O
|
B:GLU254
|
4.3
|
24.5
|
1.0
|
CD1
|
B:TRP143
|
4.5
|
26.8
|
1.0
|
ND1
|
B:HIS260
|
4.5
|
25.0
|
1.0
|
O
|
B:TYR141
|
4.7
|
27.3
|
1.0
|
CA
|
B:HIS260
|
4.7
|
24.5
|
1.0
|
CA
|
B:CYS256
|
4.8
|
25.8
|
1.0
|
CA
|
B:CYS252
|
4.9
|
24.9
|
1.0
|
CB
|
B:MET263
|
4.9
|
24.2
|
1.0
|
|
Copper binding site 4 out
of 6 in 3omn
Go back to
Copper Binding Sites List in 3omn
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 in the Reduced State
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 in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu553
b:45.1
occ:1.00
|
NE2
|
C:HIS334
|
2.0
|
40.8
|
1.0
|
ND1
|
C:HIS284
|
2.2
|
43.8
|
1.0
|
NE2
|
C:HIS333
|
2.3
|
40.4
|
1.0
|
O
|
C:OH802
|
2.4
|
21.9
|
0.4
|
O
|
C:HOH701
|
2.7
|
10.1
|
0.4
|
CE1
|
C:HIS334
|
2.9
|
39.8
|
1.0
|
CD2
|
C:HIS334
|
3.0
|
38.6
|
1.0
|
CG
|
C:HIS284
|
3.1
|
43.1
|
1.0
|
CE1
|
C:HIS333
|
3.1
|
40.0
|
1.0
|
CE1
|
C:HIS284
|
3.2
|
44.1
|
1.0
|
CD2
|
C:HIS333
|
3.3
|
39.1
|
1.0
|
CB
|
C:HIS284
|
3.4
|
42.0
|
1.0
|
CA
|
C:HIS284
|
4.0
|
41.7
|
1.0
|
ND1
|
C:HIS334
|
4.0
|
39.3
|
1.0
|
CG
|
C:HIS334
|
4.1
|
38.9
|
1.0
|
CD2
|
C:HIS284
|
4.2
|
44.2
|
1.0
|
NE2
|
C:HIS284
|
4.2
|
43.5
|
1.0
|
ND1
|
C:HIS333
|
4.3
|
39.7
|
1.0
|
CG
|
C:HIS333
|
4.4
|
39.1
|
1.0
|
NA
|
C:HEA2
|
4.5
|
28.6
|
0.4
|
C4A
|
C:HEA2
|
4.6
|
28.6
|
0.4
|
FE
|
C:HEA2
|
4.7
|
27.4
|
0.4
|
C1A
|
C:HEA2
|
4.7
|
27.9
|
0.4
|
ND
|
C:HEA2
|
4.7
|
39.3
|
0.6
|
N
|
C:HIS284
|
4.8
|
41.4
|
1.0
|
CG2
|
C:VAL287
|
4.8
|
40.1
|
1.0
|
C1A
|
C:HEA2
|
4.8
|
39.4
|
0.6
|
C4D
|
C:HEA2
|
4.8
|
39.5
|
0.6
|
NB
|
C:HEA2
|
4.9
|
29.5
|
0.4
|
NA
|
C:HEA2
|
4.9
|
39.8
|
0.6
|
C3A
|
C:HEA2
|
4.9
|
28.1
|
0.4
|
C2A
|
C:HEA2
|
4.9
|
28.5
|
0.4
|
CHB
|
C:HEA2
|
5.0
|
28.9
|
0.4
|
|
Copper binding site 5 out
of 6 in 3omn
Go back to
Copper Binding Sites List in 3omn
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 in the Reduced State
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 in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu286
b:33.6
occ:1.00
|
ND1
|
D:HIS260
|
2.0
|
32.0
|
1.0
|
SG
|
D:CYS256
|
2.3
|
32.6
|
1.0
|
SG
|
D:CYS252
|
2.3
|
30.2
|
1.0
|
CU
|
D:CU1287
|
2.6
|
32.8
|
1.0
|
O
|
D:GLU254
|
2.6
|
32.9
|
1.0
|
CE1
|
D:HIS260
|
2.9
|
31.6
|
1.0
|
CG
|
D:HIS260
|
3.2
|
31.6
|
1.0
|
CB
|
D:CYS252
|
3.2
|
29.8
|
1.0
|
CB
|
D:CYS256
|
3.4
|
32.7
|
1.0
|
C
|
D:GLU254
|
3.6
|
32.4
|
1.0
|
CA
|
D:HIS260
|
3.6
|
32.1
|
1.0
|
CB
|
D:HIS260
|
3.7
|
31.9
|
1.0
|
N
|
D:CYS256
|
3.7
|
33.0
|
1.0
|
O
|
D:HIS260
|
3.9
|
31.9
|
1.0
|
NE2
|
D:HIS260
|
4.0
|
31.5
|
1.0
|
N
|
D:GLU254
|
4.1
|
31.7
|
1.0
|
C
|
D:CYS252
|
4.1
|
30.4
|
1.0
|
O
|
D:CYS252
|
4.2
|
30.0
|
1.0
|
CD2
|
D:HIS260
|
4.2
|
31.7
|
1.0
|
CA
|
D:CYS256
|
4.2
|
32.8
|
1.0
|
C
|
D:HIS260
|
4.2
|
32.1
|
1.0
|
ND1
|
D:HIS217
|
4.2
|
29.0
|
1.0
|
CA
|
D:LEU255
|
4.3
|
32.9
|
1.0
|
C
|
D:LEU255
|
4.3
|
32.5
|
1.0
|
CA
|
D:CYS252
|
4.3
|
30.3
|
1.0
|
N
|
D:LEU255
|
4.3
|
32.4
|
1.0
|
CA
|
D:GLU254
|
4.5
|
32.1
|
1.0
|
SD
|
D:MET263
|
4.5
|
34.0
|
1.0
|
N
|
D:SER253
|
4.5
|
30.9
|
1.0
|
CG
|
D:MET263
|
4.7
|
32.5
|
1.0
|
N
|
D:HIS260
|
4.8
|
33.0
|
1.0
|
CA
|
D:HIS217
|
4.9
|
31.9
|
1.0
|
|
Copper binding site 6 out
of 6 in 3omn
Go back to
Copper Binding Sites List in 3omn
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 in the Reduced State
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 in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu287
b:32.8
occ:1.00
|
ND1
|
D:HIS217
|
2.0
|
29.0
|
1.0
|
SG
|
D:CYS256
|
2.3
|
32.6
|
1.0
|
SG
|
D:CYS252
|
2.3
|
30.2
|
1.0
|
SD
|
D:MET263
|
2.4
|
34.0
|
1.0
|
CU
|
D:CU1286
|
2.6
|
33.6
|
1.0
|
CE1
|
D:HIS217
|
2.9
|
29.4
|
1.0
|
CE
|
D:MET263
|
3.0
|
30.0
|
1.0
|
CG
|
D:HIS217
|
3.1
|
30.1
|
1.0
|
CB
|
D:CYS256
|
3.3
|
32.7
|
1.0
|
CG
|
D:MET263
|
3.4
|
32.5
|
1.0
|
CB
|
D:CYS252
|
3.4
|
29.8
|
1.0
|
CB
|
D:HIS217
|
3.5
|
32.0
|
1.0
|
NE2
|
D:HIS217
|
4.1
|
27.2
|
1.0
|
CA
|
D:HIS217
|
4.2
|
31.9
|
1.0
|
CD2
|
D:HIS217
|
4.2
|
27.4
|
1.0
|
O
|
D:GLU254
|
4.3
|
32.9
|
1.0
|
CD1
|
D:TRP143
|
4.4
|
36.7
|
1.0
|
ND1
|
D:HIS260
|
4.6
|
32.0
|
1.0
|
O
|
D:TYR141
|
4.7
|
35.9
|
1.0
|
CA
|
D:CYS256
|
4.7
|
32.8
|
1.0
|
CA
|
D:HIS260
|
4.8
|
32.1
|
1.0
|
CB
|
D:MET263
|
4.8
|
32.6
|
1.0
|
CA
|
D:CYS252
|
4.8
|
30.3
|
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 01:30:06 2024
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