Copper in PDB 1m57: Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant))
Enzymatic activity of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant))
All present enzymatic activity of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)):
1.9.3.1;
Protein crystallography data
The structure of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)), PDB code: 1m57
was solved by
M.Svensson-Ek,
J.Abramson,
G.Larsson,
S.Tornroth,
P.Brezezinski,
S.Iwata,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
4.00 /
3.00
|
Space group
|
H 3
|
Cell size a, b, c (Å), α, β, γ (°)
|
340.720,
340.720,
89.760,
90.00,
90.00,
120.00
|
R / Rfree (%)
|
29.3 /
32.9
|
Other elements in 1m57:
The structure of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)) also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant))
(pdb code 1m57). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)), PDB code: 1m57:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 1m57
Go back to
Copper Binding Sites List in 1m57
Copper binding site 1 out
of 6 in the Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant))
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu1005
b:22.8
occ:1.00
|
ND1
|
A:HIS284
|
2.1
|
15.2
|
1.0
|
NE2
|
A:HIS334
|
2.1
|
19.0
|
1.0
|
NE2
|
A:HIS333
|
2.2
|
17.6
|
1.0
|
CE1
|
A:HIS284
|
2.6
|
13.4
|
1.0
|
CD2
|
A:HIS334
|
3.0
|
17.2
|
1.0
|
CD2
|
A:HIS333
|
3.1
|
16.0
|
1.0
|
CE1
|
A:HIS333
|
3.2
|
11.7
|
1.0
|
CE1
|
A:HIS334
|
3.2
|
20.0
|
1.0
|
CG
|
A:HIS284
|
3.2
|
13.5
|
1.0
|
NE2
|
A:HIS284
|
3.8
|
17.3
|
1.0
|
CB
|
A:HIS284
|
3.8
|
12.2
|
1.0
|
CA
|
A:HIS284
|
3.9
|
9.5
|
1.0
|
CD2
|
A:HIS284
|
4.2
|
15.5
|
1.0
|
CG
|
A:HIS334
|
4.2
|
17.6
|
1.0
|
O
|
A:GLY283
|
4.2
|
12.4
|
1.0
|
ND1
|
A:HIS333
|
4.3
|
13.1
|
1.0
|
CG
|
A:HIS333
|
4.3
|
14.9
|
1.0
|
ND1
|
A:HIS334
|
4.3
|
20.0
|
1.0
|
NA
|
A:HEA1002
|
4.4
|
12.7
|
1.0
|
C1A
|
A:HEA1002
|
4.6
|
12.7
|
1.0
|
FE
|
A:HEA1002
|
4.7
|
14.6
|
1.0
|
C4A
|
A:HEA1002
|
4.7
|
13.0
|
1.0
|
CHA
|
A:HEA1002
|
4.8
|
12.9
|
1.0
|
N
|
A:HIS284
|
4.9
|
10.0
|
1.0
|
ND
|
A:HEA1002
|
4.9
|
11.6
|
1.0
|
|
Copper binding site 2 out
of 6 in 1m57
Go back to
Copper Binding Sites List in 1m57
Copper binding site 2 out
of 6 in the Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant))
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu1003
b:22.4
occ:1.00
|
ND1
|
B:HIS260
|
2.1
|
23.0
|
1.0
|
SG
|
B:CYS256
|
2.2
|
20.3
|
1.0
|
SG
|
B:CYS252
|
2.2
|
20.8
|
1.0
|
CE1
|
B:HIS260
|
2.6
|
20.9
|
1.0
|
CU
|
B:CU1004
|
2.7
|
19.8
|
1.0
|
O
|
B:GLU254
|
2.8
|
18.6
|
1.0
|
CB
|
B:CYS256
|
3.0
|
13.1
|
1.0
|
CB
|
B:CYS252
|
3.1
|
15.4
|
1.0
|
N
|
B:CYS256
|
3.3
|
14.0
|
1.0
|
CG
|
B:HIS260
|
3.4
|
19.9
|
1.0
|
C
|
B:GLU254
|
3.7
|
15.4
|
1.0
|
CA
|
B:CYS256
|
3.9
|
14.0
|
1.0
|
NE2
|
B:HIS260
|
3.9
|
22.1
|
1.0
|
CB
|
B:HIS260
|
3.9
|
14.9
|
1.0
|
CA
|
B:HIS260
|
4.0
|
13.1
|
1.0
|
N
|
B:GLU254
|
4.0
|
13.2
|
1.0
|
O
|
B:HIS260
|
4.1
|
11.8
|
1.0
|
O
|
B:CYS252
|
4.1
|
13.6
|
1.0
|
C
|
B:CYS252
|
4.2
|
13.4
|
1.0
|
C
|
B:LEU255
|
4.2
|
14.9
|
1.0
|
CD2
|
B:HIS260
|
4.2
|
21.5
|
1.0
|
N
|
B:LEU255
|
4.4
|
14.0
|
1.0
|
ND1
|
B:HIS217
|
4.4
|
21.4
|
1.0
|
CA
|
B:CYS252
|
4.4
|
14.6
|
1.0
|
CA
|
B:LEU255
|
4.4
|
13.8
|
1.0
|
C
|
B:HIS260
|
4.5
|
12.3
|
1.0
|
SD
|
B:MET263
|
4.5
|
2.0
|
1.0
|
CA
|
B:GLU254
|
4.5
|
14.7
|
1.0
|
N
|
B:SER253
|
4.5
|
13.1
|
1.0
|
C
|
B:CYS256
|
4.7
|
15.3
|
1.0
|
C
|
B:SER253
|
4.9
|
12.0
|
1.0
|
CB
|
B:HIS217
|
5.0
|
17.8
|
1.0
|
|
Copper binding site 3 out
of 6 in 1m57
Go back to
Copper Binding Sites List in 1m57
Copper binding site 3 out
of 6 in the Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant))
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu1004
b:19.8
occ:1.00
|
ND1
|
B:HIS217
|
2.1
|
21.4
|
1.0
|
SG
|
B:CYS252
|
2.3
|
20.8
|
1.0
|
SG
|
B:CYS256
|
2.3
|
20.3
|
1.0
|
SD
|
B:MET263
|
2.6
|
2.0
|
1.0
|
CU
|
B:CU1003
|
2.7
|
22.4
|
1.0
|
CE1
|
B:HIS217
|
3.0
|
22.0
|
1.0
|
CB
|
B:CYS256
|
3.0
|
13.1
|
1.0
|
CG
|
B:HIS217
|
3.2
|
19.3
|
1.0
|
CB
|
B:HIS217
|
3.5
|
17.8
|
1.0
|
CB
|
B:CYS252
|
3.5
|
15.4
|
1.0
|
CE
|
B:MET263
|
3.9
|
2.0
|
1.0
|
CG
|
B:MET263
|
4.0
|
2.0
|
1.0
|
NE2
|
B:HIS217
|
4.2
|
22.6
|
1.0
|
CD2
|
B:HIS217
|
4.3
|
19.5
|
1.0
|
CA
|
B:HIS217
|
4.3
|
16.6
|
1.0
|
CA
|
B:CYS256
|
4.5
|
14.0
|
1.0
|
O
|
B:GLU254
|
4.6
|
18.6
|
1.0
|
ND1
|
B:HIS260
|
4.7
|
23.0
|
1.0
|
N
|
B:CYS256
|
4.8
|
14.0
|
1.0
|
CA
|
B:CYS252
|
4.9
|
14.6
|
1.0
|
O
|
B:CYS256
|
4.9
|
16.7
|
1.0
|
CD1
|
B:TRP143
|
4.9
|
20.6
|
1.0
|
|
Copper binding site 4 out
of 6 in 1m57
Go back to
Copper Binding Sites List in 1m57
Copper binding site 4 out
of 6 in the Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant))
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Cu1005
b:24.2
occ:1.00
|
ND1
|
G:HIS284
|
2.1
|
16.2
|
1.0
|
NE2
|
G:HIS334
|
2.1
|
19.5
|
1.0
|
NE2
|
G:HIS333
|
2.2
|
18.1
|
1.0
|
CD2
|
G:HIS334
|
2.7
|
16.9
|
1.0
|
CE1
|
G:HIS284
|
2.8
|
14.0
|
1.0
|
CD2
|
G:HIS333
|
2.9
|
16.3
|
1.0
|
CE1
|
G:HIS333
|
3.1
|
11.3
|
1.0
|
CG
|
G:HIS284
|
3.2
|
15.0
|
1.0
|
CE1
|
G:HIS334
|
3.3
|
20.2
|
1.0
|
CB
|
G:HIS284
|
3.7
|
12.8
|
1.0
|
NE2
|
G:HIS284
|
3.9
|
17.8
|
1.0
|
CG
|
G:HIS333
|
4.0
|
15.5
|
1.0
|
CA
|
G:HIS284
|
4.0
|
10.1
|
1.0
|
CG
|
G:HIS334
|
4.0
|
17.6
|
1.0
|
ND1
|
G:HIS333
|
4.0
|
12.8
|
1.0
|
CD2
|
G:HIS284
|
4.2
|
16.2
|
1.0
|
ND1
|
G:HIS334
|
4.3
|
20.2
|
1.0
|
O
|
G:GLY283
|
4.5
|
13.4
|
1.0
|
NA
|
G:HEA1002
|
4.7
|
12.8
|
1.0
|
CE3
|
G:TRP280
|
4.8
|
6.3
|
1.0
|
C1A
|
G:HEA1002
|
4.9
|
12.9
|
1.0
|
C4A
|
G:HEA1002
|
4.9
|
13.1
|
1.0
|
N
|
G:HIS284
|
4.9
|
10.2
|
1.0
|
|
Copper binding site 5 out
of 6 in 1m57
Go back to
Copper Binding Sites List in 1m57
Copper binding site 5 out
of 6 in the Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant))
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Cu1003
b:25.5
occ:1.00
|
ND1
|
H:HIS260
|
2.1
|
23.0
|
1.0
|
SG
|
H:CYS256
|
2.3
|
21.8
|
1.0
|
SG
|
H:CYS252
|
2.3
|
22.6
|
1.0
|
CE1
|
H:HIS260
|
2.5
|
20.8
|
1.0
|
CU
|
H:CU1004
|
2.7
|
22.7
|
1.0
|
O
|
H:GLU254
|
2.8
|
18.9
|
1.0
|
CB
|
H:CYS252
|
2.9
|
15.9
|
1.0
|
CB
|
H:CYS256
|
3.1
|
13.4
|
1.0
|
CG
|
H:HIS260
|
3.3
|
19.8
|
1.0
|
N
|
H:CYS256
|
3.5
|
15.3
|
1.0
|
O
|
H:HIS260
|
3.6
|
12.6
|
1.0
|
CA
|
H:HIS260
|
3.6
|
12.9
|
1.0
|
NE2
|
H:HIS260
|
3.8
|
22.4
|
1.0
|
C
|
H:GLU254
|
3.8
|
15.7
|
1.0
|
CB
|
H:HIS260
|
3.8
|
14.5
|
1.0
|
N
|
H:GLU254
|
3.9
|
14.1
|
1.0
|
CA
|
H:CYS256
|
3.9
|
14.7
|
1.0
|
C
|
H:HIS260
|
4.1
|
13.2
|
1.0
|
CD2
|
H:HIS260
|
4.2
|
21.7
|
1.0
|
C
|
H:CYS252
|
4.2
|
13.6
|
1.0
|
CA
|
H:CYS252
|
4.3
|
14.8
|
1.0
|
N
|
H:SER253
|
4.3
|
13.3
|
1.0
|
SD
|
H:MET263
|
4.4
|
2.0
|
1.0
|
ND1
|
H:HIS217
|
4.4
|
21.4
|
1.0
|
C
|
H:LEU255
|
4.4
|
15.7
|
1.0
|
O
|
H:CYS252
|
4.4
|
13.6
|
1.0
|
CA
|
H:GLU254
|
4.5
|
15.4
|
1.0
|
CA
|
H:LEU255
|
4.6
|
14.2
|
1.0
|
N
|
H:LEU255
|
4.6
|
14.1
|
1.0
|
C
|
H:CYS256
|
4.7
|
15.5
|
1.0
|
CB
|
H:HIS217
|
4.8
|
17.1
|
1.0
|
N
|
H:HIS260
|
4.9
|
13.1
|
1.0
|
CG
|
H:MET263
|
4.9
|
2.4
|
1.0
|
C
|
H:SER253
|
4.9
|
12.7
|
1.0
|
|
Copper binding site 6 out
of 6 in 1m57
Go back to
Copper Binding Sites List in 1m57
Copper binding site 6 out
of 6 in the Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant))
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Structure of Cytochrome C Oxidase From Rhodobacter Sphaeroides (Eq(I-286) Mutant)) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Cu1004
b:22.7
occ:1.00
|
ND1
|
H:HIS217
|
2.1
|
21.4
|
1.0
|
SG
|
H:CYS252
|
2.3
|
22.6
|
1.0
|
SG
|
H:CYS256
|
2.4
|
21.8
|
1.0
|
SD
|
H:MET263
|
2.6
|
2.0
|
1.0
|
CU
|
H:CU1003
|
2.7
|
25.5
|
1.0
|
CG
|
H:HIS217
|
2.8
|
19.6
|
1.0
|
CB
|
H:CYS256
|
2.9
|
13.4
|
1.0
|
CB
|
H:HIS217
|
2.9
|
17.1
|
1.0
|
CE1
|
H:HIS217
|
3.1
|
21.4
|
1.0
|
CB
|
H:CYS252
|
3.3
|
15.9
|
1.0
|
CA
|
H:HIS217
|
3.9
|
16.5
|
1.0
|
CD2
|
H:HIS217
|
4.0
|
20.4
|
1.0
|
NE2
|
H:HIS217
|
4.1
|
23.0
|
1.0
|
CG
|
H:MET263
|
4.1
|
2.4
|
1.0
|
CE
|
H:MET263
|
4.2
|
2.0
|
1.0
|
O
|
H:GLU254
|
4.2
|
18.9
|
1.0
|
CA
|
H:CYS256
|
4.4
|
14.7
|
1.0
|
ND1
|
H:HIS260
|
4.7
|
23.0
|
1.0
|
CA
|
H:CYS252
|
4.7
|
14.8
|
1.0
|
O
|
H:CYS256
|
4.8
|
16.0
|
1.0
|
N
|
H:SER218
|
4.8
|
16.2
|
1.0
|
N
|
H:CYS256
|
4.8
|
15.3
|
1.0
|
O
|
H:ILE216
|
4.9
|
20.4
|
1.0
|
C
|
H:HIS217
|
4.9
|
16.7
|
1.0
|
N
|
H:HIS217
|
4.9
|
16.3
|
1.0
|
C
|
H:CYS256
|
5.0
|
15.5
|
1.0
|
|
Reference:
M.Svensson-Ek,
J.Abramson,
G.Larsson,
S.Tornroth,
P.Brzezinski,
S.Iwata.
The X-Ray Crystal Structures of Wild-Type and Eq(I-286) Mutant Cytochrome C Oxidases From Rhodobacter Sphaeroides. J.Mol.Biol. V. 321 329 2002.
ISSN: ISSN 0022-2836
PubMed: 12144789
DOI: 10.1016/S0022-2836(02)00619-8
Page generated: Tue Jul 30 22:20:03 2024
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