Copper in PDB 1pu0: Structure of Human Cu,Zn Superoxide Dismutase
Enzymatic activity of Structure of Human Cu,Zn Superoxide Dismutase
All present enzymatic activity of Structure of Human Cu,Zn Superoxide Dismutase:
1.15.1.1;
Protein crystallography data
The structure of Structure of Human Cu,Zn Superoxide Dismutase, PDB code: 1pu0
was solved by
M.Didonato,
L.Craig,
M.E.Huff,
M.M.Thayer,
R.M.F.Cardoso,
C.J.Kassmann,
T.P.Lo,
C.K.Bruns,
E.T.Powers,
J.W.Kelly,
E.D.Getzoff,
J.A.Tainer,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
1.70
|
Space group
|
C 2 2 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
203.580,
165.680,
144.150,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
21 /
24.3
|
Other elements in 1pu0:
The structure of Structure of Human Cu,Zn Superoxide Dismutase also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Structure of Human Cu,Zn Superoxide Dismutase
(pdb code 1pu0). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 10 binding sites of Copper where determined in the
Structure of Human Cu,Zn Superoxide Dismutase, PDB code: 1pu0:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Copper binding site 1 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 1 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu200
b:24.4
occ:1.00
|
NE2
|
A:HIS48
|
2.0
|
21.0
|
1.0
|
NE2
|
A:HIS120
|
2.1
|
20.3
|
1.0
|
ND1
|
A:HIS46
|
2.1
|
25.5
|
1.0
|
CD2
|
A:HIS120
|
2.9
|
29.7
|
1.0
|
CE1
|
A:HIS48
|
2.9
|
24.3
|
1.0
|
CE1
|
A:HIS46
|
3.1
|
28.6
|
1.0
|
CG
|
A:HIS46
|
3.1
|
28.2
|
1.0
|
CD2
|
A:HIS48
|
3.1
|
18.6
|
1.0
|
CE1
|
A:HIS120
|
3.2
|
24.7
|
1.0
|
NE2
|
A:HIS63
|
3.3
|
34.3
|
1.0
|
CB
|
A:HIS46
|
3.5
|
23.0
|
1.0
|
CD2
|
A:HIS63
|
3.6
|
32.1
|
1.0
|
CB
|
A:VAL118
|
3.9
|
22.8
|
1.0
|
ND1
|
A:HIS48
|
4.1
|
22.3
|
1.0
|
CG
|
A:HIS120
|
4.1
|
27.8
|
1.0
|
CG
|
A:HIS48
|
4.2
|
23.4
|
1.0
|
NE2
|
A:HIS46
|
4.2
|
24.3
|
1.0
|
CG1
|
A:VAL118
|
4.2
|
22.4
|
1.0
|
ND1
|
A:HIS120
|
4.2
|
23.2
|
1.0
|
CD2
|
A:HIS46
|
4.2
|
23.7
|
1.0
|
N
|
A:HIS46
|
4.2
|
23.0
|
1.0
|
CE1
|
A:HIS63
|
4.3
|
27.6
|
1.0
|
CA
|
A:HIS46
|
4.3
|
22.3
|
1.0
|
O
|
A:HOH400
|
4.4
|
34.9
|
1.0
|
O
|
A:VAL118
|
4.6
|
21.3
|
1.0
|
O
|
A:HIS46
|
4.6
|
20.6
|
1.0
|
CG2
|
A:VAL118
|
4.6
|
20.7
|
1.0
|
CG
|
A:HIS63
|
4.7
|
29.1
|
1.0
|
C
|
A:HIS46
|
4.7
|
28.6
|
1.0
|
C
|
A:VAL118
|
5.0
|
23.0
|
1.0
|
|
Copper binding site 2 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 2 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu200
b:21.1
occ:1.00
|
NE2
|
B:HIS48
|
2.0
|
20.0
|
1.0
|
ND1
|
B:HIS46
|
2.0
|
20.3
|
1.0
|
NE2
|
B:HIS120
|
2.0
|
23.9
|
1.0
|
CE1
|
B:HIS48
|
2.9
|
21.1
|
1.0
|
CD2
|
B:HIS120
|
3.0
|
25.8
|
1.0
|
CG
|
B:HIS46
|
3.0
|
22.5
|
1.0
|
CE1
|
B:HIS46
|
3.0
|
21.5
|
1.0
|
CD2
|
B:HIS48
|
3.1
|
20.1
|
1.0
|
CE1
|
B:HIS120
|
3.1
|
20.4
|
1.0
|
NE2
|
B:HIS63
|
3.3
|
21.7
|
1.0
|
CB
|
B:HIS46
|
3.3
|
20.7
|
1.0
|
CD2
|
B:HIS63
|
3.6
|
25.5
|
1.0
|
O
|
B:HOH430
|
3.7
|
39.6
|
1.0
|
CB
|
B:VAL118
|
4.0
|
20.2
|
1.0
|
O
|
B:HOH401
|
4.0
|
31.4
|
1.0
|
ND1
|
B:HIS48
|
4.0
|
24.1
|
1.0
|
CG
|
B:HIS120
|
4.1
|
18.0
|
1.0
|
CG1
|
B:VAL118
|
4.1
|
17.7
|
1.0
|
CD2
|
B:HIS46
|
4.1
|
23.0
|
1.0
|
ND1
|
B:HIS120
|
4.2
|
17.7
|
1.0
|
NE2
|
B:HIS46
|
4.2
|
19.6
|
1.0
|
CG
|
B:HIS48
|
4.2
|
21.3
|
1.0
|
N
|
B:HIS46
|
4.2
|
17.8
|
1.0
|
CE1
|
B:HIS63
|
4.3
|
21.8
|
1.0
|
CA
|
B:HIS46
|
4.3
|
18.8
|
1.0
|
O
|
B:VAL118
|
4.5
|
18.0
|
1.0
|
O
|
B:HIS46
|
4.5
|
18.8
|
1.0
|
CG2
|
B:VAL118
|
4.7
|
20.4
|
1.0
|
C
|
B:HIS46
|
4.7
|
19.1
|
1.0
|
CG
|
B:HIS63
|
4.7
|
17.8
|
1.0
|
C
|
B:VAL118
|
5.0
|
19.9
|
1.0
|
ND1
|
B:HIS63
|
5.0
|
19.2
|
1.0
|
|
Copper binding site 3 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 3 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu200
b:40.6
occ:1.00
|
NE2
|
C:HIS120
|
2.0
|
31.0
|
1.0
|
NE2
|
C:HIS48
|
2.0
|
23.4
|
1.0
|
ND1
|
C:HIS46
|
2.0
|
51.2
|
1.0
|
CD2
|
C:HIS120
|
2.9
|
27.4
|
1.0
|
CE1
|
C:HIS48
|
2.9
|
24.1
|
1.0
|
CD2
|
C:HIS48
|
3.0
|
30.8
|
1.0
|
CE1
|
C:HIS46
|
3.0
|
56.3
|
1.0
|
CE1
|
C:HIS120
|
3.0
|
36.8
|
1.0
|
CG
|
C:HIS46
|
3.0
|
45.8
|
1.0
|
CB
|
C:HIS46
|
3.4
|
26.2
|
1.0
|
NE2
|
C:HIS63
|
3.5
|
50.6
|
1.0
|
CD2
|
C:HIS63
|
3.9
|
46.2
|
1.0
|
CB
|
C:VAL118
|
4.0
|
29.0
|
1.0
|
CG
|
C:HIS120
|
4.0
|
33.2
|
1.0
|
ND1
|
C:HIS48
|
4.0
|
29.3
|
1.0
|
CE1
|
C:HIS63
|
4.1
|
51.8
|
1.0
|
ND1
|
C:HIS120
|
4.1
|
30.6
|
1.0
|
CG
|
C:HIS48
|
4.1
|
27.1
|
1.0
|
NE2
|
C:HIS46
|
4.1
|
45.6
|
1.0
|
CD2
|
C:HIS46
|
4.1
|
46.0
|
1.0
|
CG1
|
C:VAL118
|
4.2
|
35.8
|
1.0
|
O
|
C:HOH402
|
4.2
|
44.0
|
1.0
|
N
|
C:HIS46
|
4.3
|
36.1
|
1.0
|
CA
|
C:HIS46
|
4.4
|
26.4
|
1.0
|
CG2
|
C:VAL118
|
4.6
|
28.6
|
1.0
|
O
|
C:VAL118
|
4.7
|
34.1
|
1.0
|
CG
|
C:HIS63
|
4.7
|
44.7
|
1.0
|
ND1
|
C:HIS63
|
4.7
|
45.6
|
1.0
|
O
|
C:HIS46
|
4.8
|
32.5
|
1.0
|
C
|
C:HIS46
|
4.8
|
37.6
|
1.0
|
|
Copper binding site 4 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 4 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu200
b:22.9
occ:1.00
|
NE2
|
D:HIS48
|
2.0
|
24.5
|
1.0
|
NE2
|
D:HIS120
|
2.0
|
19.9
|
1.0
|
ND1
|
D:HIS46
|
2.0
|
21.1
|
1.0
|
CD2
|
D:HIS120
|
2.9
|
19.4
|
1.0
|
CE1
|
D:HIS48
|
3.0
|
25.2
|
1.0
|
CE1
|
D:HIS46
|
3.0
|
22.2
|
1.0
|
CD2
|
D:HIS48
|
3.0
|
23.1
|
1.0
|
CG
|
D:HIS46
|
3.0
|
23.3
|
1.0
|
CE1
|
D:HIS120
|
3.0
|
21.4
|
1.0
|
CB
|
D:HIS46
|
3.4
|
17.9
|
1.0
|
NE2
|
D:HIS63
|
3.4
|
27.0
|
1.0
|
O
|
D:HOH403
|
3.7
|
29.8
|
1.0
|
CD2
|
D:HIS63
|
3.8
|
24.0
|
1.0
|
CB
|
D:VAL118
|
3.9
|
19.0
|
1.0
|
CG1
|
D:VAL118
|
4.1
|
20.8
|
1.0
|
ND1
|
D:HIS48
|
4.1
|
20.0
|
1.0
|
CG
|
D:HIS120
|
4.1
|
19.8
|
1.0
|
NE2
|
D:HIS46
|
4.1
|
21.9
|
1.0
|
ND1
|
D:HIS120
|
4.1
|
18.4
|
1.0
|
CG
|
D:HIS48
|
4.1
|
21.1
|
1.0
|
CD2
|
D:HIS46
|
4.1
|
22.6
|
1.0
|
N
|
D:HIS46
|
4.2
|
18.9
|
1.0
|
CA
|
D:HIS46
|
4.3
|
17.3
|
1.0
|
CE1
|
D:HIS63
|
4.3
|
19.6
|
1.0
|
O
|
D:VAL118
|
4.5
|
20.8
|
1.0
|
O
|
D:HIS46
|
4.5
|
20.7
|
1.0
|
C
|
D:HIS46
|
4.6
|
21.9
|
1.0
|
CG2
|
D:VAL118
|
4.7
|
22.1
|
1.0
|
CG
|
D:HIS63
|
4.8
|
23.7
|
1.0
|
C
|
D:VAL118
|
5.0
|
22.3
|
1.0
|
|
Copper binding site 5 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 5 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Cu200
b:22.5
occ:1.00
|
NE2
|
E:HIS48
|
2.0
|
20.8
|
1.0
|
ND1
|
E:HIS46
|
2.0
|
19.8
|
1.0
|
NE2
|
E:HIS120
|
2.0
|
21.2
|
1.0
|
CD2
|
E:HIS120
|
2.9
|
19.3
|
1.0
|
CD2
|
E:HIS48
|
3.0
|
23.4
|
1.0
|
CG
|
E:HIS46
|
3.0
|
19.3
|
1.0
|
CE1
|
E:HIS48
|
3.0
|
20.6
|
1.0
|
CE1
|
E:HIS46
|
3.0
|
21.4
|
1.0
|
CE1
|
E:HIS120
|
3.1
|
27.1
|
1.0
|
CB
|
E:HIS46
|
3.3
|
20.9
|
1.0
|
NE2
|
E:HIS63
|
3.3
|
25.6
|
1.0
|
CD2
|
E:HIS63
|
3.7
|
23.7
|
1.0
|
O
|
E:HOH1129
|
3.8
|
30.9
|
1.0
|
CB
|
E:VAL118
|
3.9
|
20.3
|
1.0
|
ND1
|
E:HIS48
|
4.1
|
22.5
|
1.0
|
CG
|
E:HIS48
|
4.1
|
20.5
|
1.0
|
NE2
|
E:HIS46
|
4.1
|
25.3
|
1.0
|
CG
|
E:HIS120
|
4.1
|
19.9
|
1.0
|
CD2
|
E:HIS46
|
4.1
|
24.6
|
1.0
|
ND1
|
E:HIS120
|
4.1
|
21.3
|
1.0
|
CG1
|
E:VAL118
|
4.1
|
22.3
|
1.0
|
N
|
E:HIS46
|
4.2
|
19.6
|
1.0
|
CE1
|
E:HIS63
|
4.2
|
26.2
|
1.0
|
CA
|
E:HIS46
|
4.2
|
22.1
|
1.0
|
O
|
E:HIS46
|
4.5
|
20.2
|
1.0
|
O
|
E:VAL118
|
4.5
|
20.0
|
1.0
|
C
|
E:HIS46
|
4.6
|
23.0
|
1.0
|
CG2
|
E:VAL118
|
4.7
|
20.7
|
1.0
|
CG
|
E:HIS63
|
4.7
|
25.0
|
1.0
|
ND1
|
E:HIS63
|
5.0
|
25.7
|
1.0
|
C
|
E:VAL118
|
5.0
|
22.8
|
1.0
|
|
Copper binding site 6 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 6 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Cu200
b:21.4
occ:1.00
|
NE2
|
F:HIS48
|
2.0
|
16.6
|
1.0
|
NE2
|
F:HIS120
|
2.0
|
19.5
|
1.0
|
ND1
|
F:HIS46
|
2.1
|
22.4
|
1.0
|
CD2
|
F:HIS120
|
2.9
|
17.5
|
1.0
|
CE1
|
F:HIS48
|
2.9
|
19.7
|
1.0
|
CD2
|
F:HIS48
|
3.0
|
19.3
|
1.0
|
CG
|
F:HIS46
|
3.0
|
18.1
|
1.0
|
CE1
|
F:HIS120
|
3.0
|
18.4
|
1.0
|
CE1
|
F:HIS46
|
3.1
|
22.2
|
1.0
|
CB
|
F:HIS46
|
3.3
|
20.8
|
1.0
|
NE2
|
F:HIS63
|
3.4
|
24.6
|
1.0
|
O
|
F:HOH404
|
3.7
|
28.3
|
1.0
|
CD2
|
F:HIS63
|
3.8
|
24.9
|
1.0
|
CB
|
F:VAL118
|
3.9
|
19.6
|
1.0
|
ND1
|
F:HIS48
|
4.0
|
18.9
|
1.0
|
CG
|
F:HIS120
|
4.1
|
17.0
|
1.0
|
ND1
|
F:HIS120
|
4.1
|
17.9
|
1.0
|
CG
|
F:HIS48
|
4.1
|
19.1
|
1.0
|
CG1
|
F:VAL118
|
4.1
|
23.2
|
1.0
|
CD2
|
F:HIS46
|
4.2
|
18.5
|
1.0
|
NE2
|
F:HIS46
|
4.2
|
21.4
|
1.0
|
N
|
F:HIS46
|
4.2
|
16.1
|
1.0
|
CE1
|
F:HIS63
|
4.2
|
21.2
|
1.0
|
CA
|
F:HIS46
|
4.3
|
16.2
|
1.0
|
O
|
F:VAL118
|
4.5
|
18.5
|
1.0
|
O
|
F:HIS46
|
4.6
|
19.5
|
1.0
|
CG2
|
F:VAL118
|
4.7
|
21.0
|
1.0
|
C
|
F:HIS46
|
4.7
|
23.6
|
1.0
|
CG
|
F:HIS63
|
4.8
|
19.4
|
1.0
|
C
|
F:VAL118
|
5.0
|
21.5
|
1.0
|
|
Copper binding site 7 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 7 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 7 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Cu200
b:35.6
occ:1.00
|
ND1
|
G:HIS46
|
1.9
|
41.6
|
1.0
|
NE2
|
G:HIS120
|
2.0
|
30.9
|
1.0
|
NE2
|
G:HIS48
|
2.1
|
35.7
|
1.0
|
CD2
|
G:HIS120
|
2.9
|
31.2
|
1.0
|
CG
|
G:HIS46
|
2.9
|
42.8
|
1.0
|
CE1
|
G:HIS46
|
3.0
|
44.0
|
1.0
|
CE1
|
G:HIS120
|
3.0
|
37.9
|
1.0
|
CE1
|
G:HIS48
|
3.1
|
30.4
|
1.0
|
CD2
|
G:HIS48
|
3.1
|
29.6
|
1.0
|
CB
|
G:HIS46
|
3.3
|
33.6
|
1.0
|
NE2
|
G:HIS63
|
3.5
|
40.0
|
1.0
|
O
|
G:HOH1467
|
3.5
|
48.2
|
1.0
|
CD2
|
G:HIS63
|
3.7
|
33.8
|
1.0
|
CB
|
G:VAL118
|
4.0
|
26.9
|
1.0
|
CG
|
G:HIS120
|
4.1
|
28.4
|
1.0
|
NE2
|
G:HIS46
|
4.1
|
39.6
|
1.0
|
ND1
|
G:HIS120
|
4.1
|
36.6
|
1.0
|
CD2
|
G:HIS46
|
4.1
|
37.6
|
1.0
|
CG1
|
G:VAL118
|
4.1
|
29.5
|
1.0
|
N
|
G:HIS46
|
4.1
|
30.4
|
1.0
|
O
|
G:HOH405
|
4.1
|
40.4
|
1.0
|
ND1
|
G:HIS48
|
4.2
|
31.2
|
1.0
|
CA
|
G:HIS46
|
4.2
|
29.0
|
1.0
|
CG
|
G:HIS48
|
4.2
|
22.9
|
1.0
|
CE1
|
G:HIS63
|
4.4
|
42.9
|
1.0
|
O
|
G:VAL118
|
4.4
|
28.2
|
1.0
|
O
|
G:HIS46
|
4.5
|
27.8
|
1.0
|
C
|
G:HIS46
|
4.6
|
43.8
|
1.0
|
CG
|
G:HIS63
|
4.7
|
38.0
|
1.0
|
CG2
|
G:VAL118
|
4.7
|
35.5
|
1.0
|
C
|
G:VAL118
|
4.9
|
30.9
|
1.0
|
C
|
G:PHE45
|
5.0
|
42.3
|
1.0
|
CA
|
G:VAL118
|
5.0
|
22.1
|
1.0
|
|
Copper binding site 8 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 8 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 8 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Cu200
b:25.9
occ:1.00
|
ND1
|
H:HIS46
|
2.0
|
23.1
|
1.0
|
NE2
|
H:HIS48
|
2.0
|
23.9
|
1.0
|
NE2
|
H:HIS120
|
2.0
|
21.7
|
1.0
|
CE1
|
H:HIS46
|
2.9
|
25.8
|
1.0
|
CD2
|
H:HIS120
|
3.0
|
21.8
|
1.0
|
CE1
|
H:HIS48
|
3.0
|
28.5
|
1.0
|
CD2
|
H:HIS48
|
3.0
|
24.4
|
1.0
|
CE1
|
H:HIS120
|
3.0
|
23.0
|
1.0
|
CG
|
H:HIS46
|
3.0
|
23.9
|
1.0
|
NE2
|
H:HIS63
|
3.3
|
29.1
|
1.0
|
CB
|
H:HIS46
|
3.4
|
24.6
|
1.0
|
CD2
|
H:HIS63
|
3.7
|
27.9
|
1.0
|
CB
|
H:VAL118
|
4.0
|
25.2
|
1.0
|
NE2
|
H:HIS46
|
4.1
|
25.0
|
1.0
|
ND1
|
H:HIS120
|
4.1
|
23.5
|
1.0
|
ND1
|
H:HIS48
|
4.1
|
24.4
|
1.0
|
CG
|
H:HIS120
|
4.1
|
26.1
|
1.0
|
CD2
|
H:HIS46
|
4.1
|
22.8
|
1.0
|
CG1
|
H:VAL118
|
4.1
|
22.8
|
1.0
|
CG
|
H:HIS48
|
4.2
|
20.9
|
1.0
|
O
|
H:HOH406
|
4.2
|
42.8
|
1.0
|
N
|
H:HIS46
|
4.2
|
20.9
|
1.0
|
CE1
|
H:HIS63
|
4.2
|
29.9
|
1.0
|
CA
|
H:HIS46
|
4.3
|
23.1
|
1.0
|
O
|
H:VAL118
|
4.5
|
24.9
|
1.0
|
O
|
H:HIS46
|
4.5
|
23.4
|
1.0
|
C
|
H:HIS46
|
4.7
|
26.3
|
1.0
|
CG
|
H:HIS63
|
4.7
|
29.2
|
1.0
|
CG2
|
H:VAL118
|
4.7
|
29.1
|
1.0
|
C
|
H:VAL118
|
5.0
|
24.0
|
1.0
|
ND1
|
H:HIS63
|
5.0
|
28.7
|
1.0
|
|
Copper binding site 9 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 9 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 9 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Cu200
b:35.8
occ:1.00
|
NE2
|
I:HIS120
|
2.0
|
31.9
|
1.0
|
ND1
|
I:HIS46
|
2.0
|
32.0
|
1.0
|
NE2
|
I:HIS48
|
2.0
|
35.7
|
1.0
|
CD2
|
I:HIS120
|
2.9
|
30.7
|
1.0
|
CG
|
I:HIS46
|
2.9
|
33.6
|
1.0
|
CE1
|
I:HIS48
|
2.9
|
32.0
|
1.0
|
CE1
|
I:HIS46
|
3.0
|
29.9
|
1.0
|
CE1
|
I:HIS120
|
3.0
|
31.5
|
1.0
|
CD2
|
I:HIS48
|
3.1
|
31.9
|
1.0
|
CB
|
I:HIS46
|
3.3
|
26.8
|
1.0
|
NE2
|
I:HIS63
|
3.5
|
34.5
|
1.0
|
CD2
|
I:HIS63
|
3.8
|
33.0
|
1.0
|
CB
|
I:VAL118
|
4.0
|
31.3
|
1.0
|
CG
|
I:HIS120
|
4.1
|
30.8
|
1.0
|
CD2
|
I:HIS46
|
4.1
|
31.7
|
1.0
|
NE2
|
I:HIS46
|
4.1
|
26.3
|
1.0
|
ND1
|
I:HIS48
|
4.1
|
32.8
|
1.0
|
ND1
|
I:HIS120
|
4.1
|
36.9
|
1.0
|
N
|
I:HIS46
|
4.1
|
28.1
|
1.0
|
CG
|
I:HIS48
|
4.2
|
33.7
|
1.0
|
CA
|
I:HIS46
|
4.2
|
28.5
|
1.0
|
CG1
|
I:VAL118
|
4.3
|
23.4
|
1.0
|
CE1
|
I:HIS63
|
4.3
|
33.5
|
1.0
|
O
|
I:VAL118
|
4.5
|
27.5
|
1.0
|
O
|
I:HIS46
|
4.5
|
27.3
|
1.0
|
CG2
|
I:VAL118
|
4.6
|
30.8
|
1.0
|
C
|
I:HIS46
|
4.7
|
30.4
|
1.0
|
CG
|
I:HIS63
|
4.8
|
36.2
|
1.0
|
C
|
I:VAL118
|
5.0
|
24.2
|
1.0
|
|
Copper binding site 10 out
of 10 in 1pu0
Go back to
Copper Binding Sites List in 1pu0
Copper binding site 10 out
of 10 in the Structure of Human Cu,Zn Superoxide Dismutase
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 10 of Structure of Human Cu,Zn Superoxide Dismutase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Cu200
b:24.9
occ:1.00
|
NE2
|
J:HIS48
|
2.0
|
24.5
|
1.0
|
NE2
|
J:HIS120
|
2.1
|
22.6
|
1.0
|
ND1
|
J:HIS46
|
2.1
|
23.0
|
1.0
|
CD2
|
J:HIS48
|
2.9
|
23.5
|
1.0
|
CE1
|
J:HIS48
|
3.0
|
27.5
|
1.0
|
CD2
|
J:HIS120
|
3.0
|
22.0
|
1.0
|
CE1
|
J:HIS46
|
3.1
|
29.5
|
1.0
|
CG
|
J:HIS46
|
3.1
|
26.1
|
1.0
|
CE1
|
J:HIS120
|
3.1
|
24.4
|
1.0
|
NE2
|
J:HIS63
|
3.2
|
29.1
|
1.0
|
CB
|
J:HIS46
|
3.4
|
20.7
|
1.0
|
CD2
|
J:HIS63
|
3.6
|
27.0
|
1.0
|
O
|
J:HOH429
|
3.7
|
49.6
|
1.0
|
O
|
J:HOH408
|
3.8
|
39.3
|
1.0
|
CB
|
J:VAL118
|
4.0
|
23.8
|
1.0
|
CG1
|
J:VAL118
|
4.0
|
27.3
|
1.0
|
ND1
|
J:HIS48
|
4.1
|
26.7
|
1.0
|
CG
|
J:HIS48
|
4.1
|
24.2
|
1.0
|
ND1
|
J:HIS120
|
4.2
|
19.7
|
1.0
|
CG
|
J:HIS120
|
4.2
|
19.2
|
1.0
|
NE2
|
J:HIS46
|
4.2
|
23.2
|
1.0
|
CD2
|
J:HIS46
|
4.2
|
21.0
|
1.0
|
N
|
J:HIS46
|
4.2
|
20.1
|
1.0
|
CE1
|
J:HIS63
|
4.2
|
26.4
|
1.0
|
CA
|
J:HIS46
|
4.3
|
21.1
|
1.0
|
O
|
J:HIS46
|
4.5
|
22.7
|
1.0
|
O
|
J:VAL118
|
4.5
|
22.3
|
1.0
|
CG
|
J:HIS63
|
4.7
|
26.2
|
1.0
|
C
|
J:HIS46
|
4.7
|
20.9
|
1.0
|
CG2
|
J:VAL118
|
4.8
|
23.3
|
1.0
|
|
Reference:
M.Didonato,
L.Craig,
M.E.Huff,
M.M.Thayer,
R.M.F.Cardoso,
C.J.Kassmann,
T.P.Lo,
C.K.Bruns,
E.T.Powers,
J.W.Kelly,
E.D.Getzoff,
J.A.Tainer.
Als Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization J.Mol.Biol. V. 332 601 2003.
ISSN: ISSN 0022-2836
PubMed: 12963370
DOI: 10.1016/S0022-2836(03)00889-1
Page generated: Tue Jul 30 22:36:04 2024
|