Copper in PDB 3om3: Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State
Enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M Mutation in the Reduced State
All present enzymatic activity of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M 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 K362M Mutation in the Reduced State, PDB code: 3om3
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)
|
40.46 /
2.60
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
124.650,
132.365,
178.006,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.8 /
22.9
|
Other elements in 3om3:
The structure of Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M 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 K362M Mutation in the Reduced State
(pdb code 3om3). 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 K362M Mutation in the Reduced State, PDB code: 3om3:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 3om3
Go back to
Copper Binding Sites List in 3om3
Copper binding site 1 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M 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 K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu5
b:48.0
occ:1.00
|
NE2
|
A:HIS334
|
2.1
|
49.3
|
1.0
|
NE2
|
A:HIS333
|
2.1
|
48.1
|
1.0
|
ND1
|
A:HIS284
|
2.2
|
45.8
|
1.0
|
CE1
|
A:HIS333
|
2.8
|
47.6
|
1.0
|
CE1
|
A:HIS334
|
3.0
|
48.8
|
1.0
|
CD2
|
A:HIS334
|
3.0
|
48.7
|
1.0
|
CG
|
A:HIS284
|
3.0
|
44.6
|
1.0
|
CE1
|
A:HIS284
|
3.2
|
45.6
|
1.0
|
CD2
|
A:HIS333
|
3.3
|
48.0
|
1.0
|
CB
|
A:HIS284
|
3.3
|
44.1
|
1.0
|
CA
|
A:HIS284
|
4.0
|
43.9
|
1.0
|
ND1
|
A:HIS333
|
4.0
|
48.0
|
1.0
|
ND1
|
A:HIS334
|
4.1
|
47.7
|
1.0
|
CG
|
A:HIS334
|
4.1
|
48.1
|
1.0
|
CD2
|
A:HIS284
|
4.2
|
44.5
|
1.0
|
NE2
|
A:HIS284
|
4.2
|
45.4
|
1.0
|
CG
|
A:HIS333
|
4.3
|
47.6
|
1.0
|
N
|
A:HIS284
|
4.8
|
44.0
|
1.0
|
ND
|
A:HEA2
|
4.8
|
44.0
|
1.0
|
NA
|
A:HEA2
|
4.9
|
47.7
|
1.0
|
C1A
|
A:HEA2
|
4.9
|
47.2
|
1.0
|
CG2
|
A:VAL287
|
4.9
|
41.2
|
1.0
|
CG2
|
A:VAL330
|
5.0
|
48.8
|
1.0
|
C4D
|
A:HEA2
|
5.0
|
45.3
|
1.0
|
|
Copper binding site 2 out
of 6 in 3om3
Go back to
Copper Binding Sites List in 3om3
Copper binding site 2 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M 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 K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu287
b:37.0
occ:1.00
|
ND1
|
B:HIS260
|
2.0
|
32.5
|
1.0
|
SG
|
B:CYS252
|
2.3
|
35.6
|
1.0
|
SG
|
B:CYS256
|
2.3
|
35.7
|
1.0
|
CU
|
B:CU1288
|
2.6
|
34.7
|
1.0
|
O
|
B:GLU254
|
2.7
|
35.8
|
1.0
|
CE1
|
B:HIS260
|
2.8
|
31.7
|
1.0
|
CG
|
B:HIS260
|
3.1
|
33.5
|
1.0
|
CB
|
B:CYS256
|
3.3
|
34.6
|
1.0
|
CB
|
B:CYS252
|
3.3
|
34.2
|
1.0
|
CB
|
B:HIS260
|
3.6
|
34.0
|
1.0
|
CA
|
B:HIS260
|
3.6
|
34.1
|
1.0
|
C
|
B:GLU254
|
3.6
|
35.2
|
1.0
|
N
|
B:CYS256
|
3.7
|
34.9
|
1.0
|
O
|
B:HIS260
|
4.0
|
33.9
|
1.0
|
NE2
|
B:HIS260
|
4.0
|
30.6
|
1.0
|
CD2
|
B:HIS260
|
4.1
|
31.8
|
1.0
|
C
|
B:CYS252
|
4.1
|
35.0
|
1.0
|
CA
|
B:CYS256
|
4.1
|
35.1
|
1.0
|
N
|
B:GLU254
|
4.1
|
35.6
|
1.0
|
O
|
B:CYS252
|
4.1
|
34.6
|
1.0
|
CA
|
B:LEU255
|
4.2
|
34.0
|
1.0
|
C
|
B:LEU255
|
4.2
|
34.3
|
1.0
|
C
|
B:HIS260
|
4.2
|
34.0
|
1.0
|
N
|
B:LEU255
|
4.3
|
34.5
|
1.0
|
ND1
|
B:HIS217
|
4.3
|
32.7
|
1.0
|
CA
|
B:CYS252
|
4.3
|
34.7
|
1.0
|
SD
|
B:MET263
|
4.4
|
35.8
|
1.0
|
CA
|
B:GLU254
|
4.6
|
35.4
|
1.0
|
N
|
B:SER253
|
4.6
|
35.0
|
1.0
|
CG
|
B:MET263
|
4.7
|
35.5
|
1.0
|
N
|
B:HIS260
|
4.8
|
34.6
|
1.0
|
CA
|
B:HIS217
|
4.9
|
34.7
|
1.0
|
C
|
B:CYS256
|
5.0
|
35.4
|
1.0
|
|
Copper binding site 3 out
of 6 in 3om3
Go back to
Copper Binding Sites List in 3om3
Copper binding site 3 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M 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 K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu288
b:34.7
occ:1.00
|
ND1
|
B:HIS217
|
2.1
|
32.7
|
1.0
|
SG
|
B:CYS252
|
2.3
|
35.6
|
1.0
|
SG
|
B:CYS256
|
2.3
|
35.7
|
1.0
|
SD
|
B:MET263
|
2.4
|
35.8
|
1.0
|
CU
|
B:CU1287
|
2.6
|
37.0
|
1.0
|
CE1
|
B:HIS217
|
3.0
|
31.8
|
1.0
|
CE
|
B:MET263
|
3.0
|
32.2
|
1.0
|
CG
|
B:HIS217
|
3.2
|
33.5
|
1.0
|
CB
|
B:CYS256
|
3.3
|
34.6
|
1.0
|
CB
|
B:CYS252
|
3.4
|
34.2
|
1.0
|
CG
|
B:MET263
|
3.5
|
35.5
|
1.0
|
CB
|
B:HIS217
|
3.6
|
34.1
|
1.0
|
NE2
|
B:HIS217
|
4.2
|
33.5
|
1.0
|
CA
|
B:HIS217
|
4.2
|
34.7
|
1.0
|
CD2
|
B:HIS217
|
4.3
|
32.2
|
1.0
|
O
|
B:GLU254
|
4.4
|
35.8
|
1.0
|
ND1
|
B:HIS260
|
4.5
|
32.5
|
1.0
|
CD1
|
B:TRP143
|
4.5
|
33.4
|
1.0
|
CA
|
B:CYS256
|
4.7
|
35.1
|
1.0
|
CA
|
B:HIS260
|
4.8
|
34.1
|
1.0
|
CA
|
B:CYS252
|
4.8
|
34.7
|
1.0
|
O
|
B:TYR141
|
4.8
|
35.9
|
1.0
|
CB
|
B:MET263
|
4.9
|
35.5
|
1.0
|
O
|
B:ILE216
|
4.9
|
34.9
|
1.0
|
CZ2
|
B:TRP145
|
5.0
|
34.5
|
1.0
|
|
Copper binding site 4 out
of 6 in 3om3
Go back to
Copper Binding Sites List in 3om3
Copper binding site 4 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M 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 K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu553
b:54.8
occ:1.00
|
NE2
|
C:HIS334
|
2.2
|
55.2
|
1.0
|
NE2
|
C:HIS333
|
2.2
|
52.7
|
1.0
|
ND1
|
C:HIS284
|
2.2
|
55.2
|
1.0
|
CD2
|
C:HIS334
|
2.9
|
54.6
|
1.0
|
CE1
|
C:HIS333
|
3.0
|
52.3
|
1.0
|
CG
|
C:HIS284
|
3.0
|
53.9
|
1.0
|
CE1
|
C:HIS284
|
3.2
|
55.1
|
1.0
|
CE1
|
C:HIS334
|
3.2
|
55.0
|
1.0
|
CB
|
C:HIS284
|
3.3
|
52.8
|
1.0
|
CD2
|
C:HIS333
|
3.3
|
52.4
|
1.0
|
CA
|
C:HIS284
|
3.9
|
52.7
|
1.0
|
CG
|
C:HIS334
|
4.1
|
53.4
|
1.0
|
CD2
|
C:HIS284
|
4.2
|
54.4
|
1.0
|
ND1
|
C:HIS333
|
4.2
|
53.1
|
1.0
|
ND1
|
C:HIS334
|
4.2
|
53.8
|
1.0
|
NE2
|
C:HIS284
|
4.2
|
54.8
|
1.0
|
CG
|
C:HIS333
|
4.3
|
52.8
|
1.0
|
N
|
C:HIS284
|
4.8
|
52.4
|
1.0
|
CG2
|
C:VAL330
|
4.9
|
55.7
|
1.0
|
CG2
|
C:VAL287
|
4.9
|
50.5
|
1.0
|
C1A
|
C:HEA2
|
4.9
|
49.9
|
1.0
|
ND
|
C:HEA2
|
5.0
|
52.1
|
1.0
|
NA
|
C:HEA2
|
5.0
|
51.3
|
1.0
|
|
Copper binding site 5 out
of 6 in 3om3
Go back to
Copper Binding Sites List in 3om3
Copper binding site 5 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M 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 K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu3
b:47.8
occ:1.00
|
ND1
|
D:HIS260
|
2.0
|
46.2
|
1.0
|
SG
|
D:CYS256
|
2.3
|
46.5
|
1.0
|
SG
|
D:CYS252
|
2.3
|
44.1
|
1.0
|
CU
|
D:CU1286
|
2.6
|
44.1
|
1.0
|
O
|
D:GLU254
|
2.7
|
46.1
|
1.0
|
CE1
|
D:HIS260
|
2.8
|
45.8
|
1.0
|
CG
|
D:HIS260
|
3.1
|
45.7
|
1.0
|
CB
|
D:CYS252
|
3.3
|
44.5
|
1.0
|
CB
|
D:CYS256
|
3.4
|
45.6
|
1.0
|
CA
|
D:HIS260
|
3.6
|
44.8
|
1.0
|
C
|
D:GLU254
|
3.6
|
45.8
|
1.0
|
CB
|
D:HIS260
|
3.6
|
45.1
|
1.0
|
N
|
D:CYS256
|
3.8
|
45.4
|
1.0
|
O
|
D:HIS260
|
3.8
|
44.1
|
1.0
|
NE2
|
D:HIS260
|
4.0
|
45.0
|
1.0
|
C
|
D:HIS260
|
4.1
|
44.1
|
1.0
|
O
|
D:CYS252
|
4.1
|
44.9
|
1.0
|
CD2
|
D:HIS260
|
4.1
|
45.7
|
1.0
|
C
|
D:CYS252
|
4.1
|
45.2
|
1.0
|
N
|
D:GLU254
|
4.2
|
45.9
|
1.0
|
CA
|
D:CYS256
|
4.2
|
45.7
|
1.0
|
CA
|
D:LEU255
|
4.3
|
45.1
|
1.0
|
N
|
D:LEU255
|
4.3
|
45.3
|
1.0
|
C
|
D:LEU255
|
4.3
|
45.1
|
1.0
|
ND1
|
D:HIS217
|
4.3
|
39.4
|
1.0
|
CA
|
D:CYS252
|
4.3
|
44.8
|
1.0
|
SD
|
D:MET263
|
4.5
|
44.4
|
1.0
|
CA
|
D:GLU254
|
4.5
|
46.0
|
1.0
|
N
|
D:SER253
|
4.6
|
45.4
|
1.0
|
CG
|
D:MET263
|
4.7
|
42.6
|
1.0
|
N
|
D:HIS260
|
4.8
|
45.8
|
1.0
|
CA
|
D:HIS217
|
4.9
|
44.0
|
1.0
|
CB
|
D:HIS217
|
4.9
|
43.4
|
1.0
|
|
Copper binding site 6 out
of 6 in 3om3
Go back to
Copper Binding Sites List in 3om3
Copper binding site 6 out
of 6 in the Catalytic Core Subunits (I and II) of Cytochrome C Oxidase From Rhodobacter Sphaeroides with K362M 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 K362M Mutation in the Reduced State within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu286
b:44.1
occ:1.00
|
ND1
|
D:HIS217
|
2.1
|
39.4
|
1.0
|
SG
|
D:CYS252
|
2.3
|
44.1
|
1.0
|
SG
|
D:CYS256
|
2.4
|
46.5
|
1.0
|
SD
|
D:MET263
|
2.4
|
44.4
|
1.0
|
CU
|
D:CU13
|
2.6
|
47.8
|
1.0
|
CE1
|
D:HIS217
|
3.1
|
38.7
|
1.0
|
CG
|
D:HIS217
|
3.1
|
41.0
|
1.0
|
CE
|
D:MET263
|
3.1
|
41.4
|
1.0
|
CB
|
D:CYS256
|
3.4
|
45.6
|
1.0
|
CB
|
D:HIS217
|
3.4
|
43.4
|
1.0
|
CB
|
D:CYS252
|
3.5
|
44.5
|
1.0
|
CG
|
D:MET263
|
3.5
|
42.6
|
1.0
|
CA
|
D:HIS217
|
4.1
|
44.0
|
1.0
|
NE2
|
D:HIS217
|
4.2
|
38.5
|
1.0
|
CD2
|
D:HIS217
|
4.2
|
38.7
|
1.0
|
O
|
D:GLU254
|
4.3
|
46.1
|
1.0
|
ND1
|
D:HIS260
|
4.5
|
46.2
|
1.0
|
CD1
|
D:TRP143
|
4.6
|
48.7
|
1.0
|
O
|
D:TYR141
|
4.7
|
48.1
|
1.0
|
CA
|
D:HIS260
|
4.8
|
44.8
|
1.0
|
CA
|
D:CYS256
|
4.8
|
45.7
|
1.0
|
CB
|
D:MET263
|
4.9
|
42.6
|
1.0
|
CA
|
D:CYS252
|
4.9
|
44.8
|
1.0
|
CZ2
|
D:TRP145
|
4.9
|
46.2
|
1.0
|
O
|
D:HIS260
|
5.0
|
44.1
|
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
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