Copper in PDB 1srd: Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution
Enzymatic activity of Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution
All present enzymatic activity of Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution:
1.15.1.1;
Protein crystallography data
The structure of Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution, PDB code: 1srd
was solved by
Y.Kitagawa,
Y.Katsube,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
5.00 /
2.00
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
166.270,
45.970,
85.680,
90.00,
99.38,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Other elements in 1srd:
The structure of Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution
(pdb code 1srd). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 4 binding sites of Copper where determined in the
Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution, PDB code: 1srd:
Jump to Copper binding site number:
1;
2;
3;
4;
Copper binding site 1 out
of 4 in 1srd
Go back to
Copper Binding Sites List in 1srd
Copper binding site 1 out
of 4 in the Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution
 Mono view
 Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu155
b:13.0
occ:1.00
|
ND1
|
A:HIS46
|
2.0
|
9.3
|
1.0
|
NE2
|
A:HIS48
|
2.1
|
10.0
|
1.0
|
NE2
|
A:HIS120
|
2.1
|
9.8
|
1.0
|
NE2
|
A:HIS63
|
2.1
|
9.0
|
1.0
|
CE1
|
A:HIS120
|
2.3
|
9.8
|
1.0
|
CE1
|
A:HIS48
|
2.8
|
9.6
|
1.0
|
CD2
|
A:HIS63
|
2.8
|
8.4
|
1.0
|
CG
|
A:HIS46
|
3.0
|
8.9
|
1.0
|
CE1
|
A:HIS46
|
3.0
|
8.9
|
1.0
|
CE1
|
A:HIS63
|
3.2
|
8.7
|
1.0
|
CD2
|
A:HIS48
|
3.2
|
9.4
|
1.0
|
CD2
|
A:HIS120
|
3.3
|
9.5
|
1.0
|
CB
|
A:HIS46
|
3.3
|
8.6
|
1.0
|
ND1
|
A:HIS120
|
3.4
|
9.7
|
1.0
|
NE2
|
A:HIS46
|
4.0
|
9.0
|
1.0
|
ND1
|
A:HIS48
|
4.0
|
9.3
|
1.0
|
CG
|
A:HIS120
|
4.0
|
9.4
|
1.0
|
CG
|
A:HIS63
|
4.0
|
8.2
|
1.0
|
CD2
|
A:HIS46
|
4.1
|
8.9
|
1.0
|
CG
|
A:HIS48
|
4.2
|
9.3
|
1.0
|
ND1
|
A:HIS63
|
4.2
|
8.4
|
1.0
|
CA
|
A:HIS46
|
4.6
|
8.4
|
1.0
|
N
|
A:HIS46
|
4.7
|
8.4
|
1.0
|
CG2
|
A:THR137
|
4.8
|
10.1
|
1.0
|
|
Copper binding site 2 out
of 4 in 1srd
Go back to
Copper Binding Sites List in 1srd
Copper binding site 2 out
of 4 in the Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution
 Mono view
 Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu155
b:13.1
occ:1.00
|
NE2
|
B:HIS63
|
2.0
|
9.0
|
1.0
|
NE2
|
B:HIS120
|
2.1
|
9.8
|
1.0
|
ND1
|
B:HIS46
|
2.1
|
9.3
|
1.0
|
NE2
|
B:HIS48
|
2.1
|
10.0
|
1.0
|
CE1
|
B:HIS120
|
2.1
|
9.8
|
1.0
|
CD2
|
B:HIS63
|
2.7
|
8.4
|
1.0
|
CE1
|
B:HIS48
|
2.9
|
9.6
|
1.0
|
CG
|
B:HIS46
|
3.0
|
8.9
|
1.0
|
CE1
|
B:HIS46
|
3.1
|
9.1
|
1.0
|
CE1
|
B:HIS63
|
3.2
|
8.7
|
1.0
|
CD2
|
B:HIS48
|
3.3
|
9.4
|
1.0
|
ND1
|
B:HIS120
|
3.3
|
9.8
|
1.0
|
CB
|
B:HIS46
|
3.3
|
8.6
|
1.0
|
CD2
|
B:HIS120
|
3.3
|
9.5
|
1.0
|
CG
|
B:HIS120
|
3.9
|
9.4
|
1.0
|
CG
|
B:HIS63
|
3.9
|
8.2
|
1.0
|
ND1
|
B:HIS48
|
4.1
|
9.4
|
1.0
|
CD2
|
B:HIS46
|
4.1
|
8.9
|
1.0
|
NE2
|
B:HIS46
|
4.1
|
9.0
|
1.0
|
ND1
|
B:HIS63
|
4.2
|
8.4
|
1.0
|
CG
|
B:HIS48
|
4.3
|
9.3
|
1.0
|
CA
|
B:HIS46
|
4.5
|
8.4
|
1.0
|
CG2
|
B:THR137
|
4.5
|
10.1
|
1.0
|
N
|
B:HIS46
|
4.7
|
8.4
|
1.0
|
O
|
B:VAL118
|
4.8
|
7.7
|
1.0
|
O
|
B:HOH178
|
4.8
|
19.0
|
1.0
|
CG1
|
B:VAL118
|
4.9
|
7.5
|
1.0
|
CB
|
B:VAL118
|
5.0
|
7.3
|
1.0
|
|
Copper binding site 3 out
of 4 in 1srd
Go back to
Copper Binding Sites List in 1srd
Copper binding site 3 out
of 4 in the Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution
 Mono view
 Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu155
b:13.5
occ:1.00
|
NE2
|
C:HIS63
|
2.0
|
9.1
|
1.0
|
NE2
|
C:HIS120
|
2.1
|
9.8
|
1.0
|
NE2
|
C:HIS48
|
2.2
|
10.0
|
1.0
|
ND1
|
C:HIS46
|
2.3
|
9.2
|
1.0
|
CE1
|
C:HIS120
|
2.3
|
9.8
|
1.0
|
CD2
|
C:HIS63
|
2.9
|
8.4
|
1.0
|
CE1
|
C:HIS48
|
2.9
|
9.6
|
1.0
|
CG
|
C:HIS46
|
3.1
|
8.8
|
1.0
|
CE1
|
C:HIS63
|
3.1
|
8.7
|
1.0
|
CD2
|
C:HIS120
|
3.2
|
9.6
|
1.0
|
CE1
|
C:HIS46
|
3.2
|
9.0
|
1.0
|
CB
|
C:HIS46
|
3.3
|
8.6
|
1.0
|
CD2
|
C:HIS48
|
3.4
|
9.4
|
1.0
|
ND1
|
C:HIS120
|
3.4
|
9.7
|
1.0
|
CG
|
C:HIS120
|
3.9
|
9.4
|
1.0
|
CG
|
C:HIS63
|
4.0
|
8.2
|
1.0
|
ND1
|
C:HIS48
|
4.1
|
9.4
|
1.0
|
CD2
|
C:HIS46
|
4.2
|
8.9
|
1.0
|
ND1
|
C:HIS63
|
4.2
|
8.4
|
1.0
|
CG2
|
C:THR137
|
4.2
|
10.2
|
1.0
|
NE2
|
C:HIS46
|
4.2
|
8.9
|
1.0
|
CG
|
C:HIS48
|
4.3
|
9.3
|
1.0
|
CA
|
C:HIS46
|
4.8
|
8.4
|
1.0
|
O
|
C:HOH175
|
4.8
|
19.0
|
1.0
|
O
|
C:THR137
|
4.9
|
9.5
|
1.0
|
|
Copper binding site 4 out
of 4 in 1srd
Go back to
Copper Binding Sites List in 1srd
Copper binding site 4 out
of 4 in the Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution
 Mono view
 Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 Angstroms Resolution within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu155
b:13.4
occ:1.00
|
NE2
|
D:HIS120
|
2.0
|
9.8
|
1.0
|
NE2
|
D:HIS48
|
2.0
|
9.9
|
1.0
|
ND1
|
D:HIS46
|
2.0
|
9.3
|
1.0
|
NE2
|
D:HIS63
|
2.1
|
9.1
|
1.0
|
CE1
|
D:HIS120
|
2.5
|
9.9
|
1.0
|
CE1
|
D:HIS48
|
2.8
|
9.6
|
1.0
|
CG
|
D:HIS46
|
2.8
|
8.8
|
1.0
|
CD2
|
D:HIS63
|
2.9
|
8.4
|
1.0
|
CD2
|
D:HIS120
|
3.0
|
9.6
|
1.0
|
CB
|
D:HIS46
|
3.1
|
8.6
|
1.0
|
CE1
|
D:HIS63
|
3.1
|
8.7
|
1.0
|
CD2
|
D:HIS48
|
3.1
|
9.4
|
1.0
|
CE1
|
D:HIS46
|
3.1
|
9.0
|
1.0
|
ND1
|
D:HIS120
|
3.6
|
9.7
|
1.0
|
ND1
|
D:HIS48
|
3.9
|
9.4
|
1.0
|
CG
|
D:HIS120
|
4.0
|
9.4
|
1.0
|
CD2
|
D:HIS46
|
4.0
|
8.9
|
1.0
|
CG
|
D:HIS63
|
4.0
|
8.2
|
1.0
|
NE2
|
D:HIS46
|
4.1
|
9.0
|
1.0
|
ND1
|
D:HIS63
|
4.1
|
8.3
|
1.0
|
CG
|
D:HIS48
|
4.1
|
9.3
|
1.0
|
CA
|
D:HIS46
|
4.4
|
8.3
|
1.0
|
N
|
D:HIS46
|
4.5
|
8.5
|
1.0
|
CB
|
D:VAL118
|
5.0
|
7.3
|
1.0
|
|
Reference:
Y.Kitagawa,
N.Tanaka,
Y.Hata,
M.Kusunoki,
G.P.Lee,
Y.Katsube,
K.Asada,
S.Aibara,
Y.Morita.
Three-Dimensional Structure of Cu,Zn-Superoxide Dismutase From Spinach at 2.0 A Resolution. J.Biochem.(Tokyo) V. 109 477 1991.
ISSN: ISSN 0021-924X
PubMed: 1880134
Page generated: Tue Jul 30 22:47:36 2024
|