Copper in PDB 7ypr: Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.
Enzymatic activity of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.
All present enzymatic activity of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.:
1.15.1.1;
Protein crystallography data
The structure of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1., PDB code: 7ypr
was solved by
K.-S.Sim,
Y.Fukuda,
T.Inoue,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
45.87 /
2.10
|
Space group
|
P 32
|
Cell size a, b, c (Å), α, β, γ (°)
|
105.825,
105.825,
76.956,
90,
90,
120
|
R / Rfree (%)
|
18 /
22.8
|
Other elements in 7ypr:
The structure of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1. also contains other interesting chemical elements:
Copper Binding Sites:
The binding sites of Copper atom in the Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.
(pdb code 7ypr). This binding sites where shown within
5.0 Angstroms radius around Copper atom.
In total 6 binding sites of Copper where determined in the
Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1., PDB code: 7ypr:
Jump to Copper binding site number:
1;
2;
3;
4;
5;
6;
Copper binding site 1 out
of 6 in 7ypr
Go back to
Copper Binding Sites List in 7ypr
Copper binding site 1 out
of 6 in the Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 1 of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Cu202
b:39.2
occ:1.00
|
NE2
|
A:HIS104
|
2.0
|
32.8
|
1.0
|
NE2
|
A:HIS162
|
2.0
|
34.4
|
1.0
|
ND1
|
A:HIS85
|
2.1
|
35.4
|
1.0
|
CE1
|
A:HIS104
|
2.8
|
25.5
|
1.0
|
O
|
A:HOH301
|
2.9
|
42.3
|
1.0
|
CD2
|
A:HIS162
|
2.9
|
31.9
|
1.0
|
CG
|
A:HIS85
|
3.0
|
29.4
|
1.0
|
CD2
|
A:HIS104
|
3.0
|
28.4
|
1.0
|
CE1
|
A:HIS162
|
3.1
|
29.2
|
1.0
|
CE1
|
A:HIS85
|
3.1
|
38.7
|
1.0
|
CB
|
A:HIS85
|
3.3
|
30.7
|
1.0
|
ND1
|
A:HIS104
|
3.9
|
24.4
|
1.0
|
CG
|
A:HIS104
|
4.1
|
36.6
|
1.0
|
CG
|
A:HIS162
|
4.1
|
31.2
|
1.0
|
ND1
|
A:HIS162
|
4.1
|
27.5
|
1.0
|
CD2
|
A:HIS85
|
4.1
|
32.3
|
1.0
|
NE2
|
A:HIS85
|
4.1
|
32.9
|
1.0
|
O
|
A:ASN179
|
4.4
|
34.9
|
1.0
|
CB
|
A:ASN179
|
4.5
|
35.8
|
1.0
|
NH1
|
A:ARG185
|
4.5
|
35.8
|
0.5
|
O
|
A:HOH365
|
4.6
|
42.6
|
1.0
|
CA
|
A:HIS85
|
4.8
|
26.8
|
1.0
|
|
Copper binding site 2 out
of 6 in 7ypr
Go back to
Copper Binding Sites List in 7ypr
Copper binding site 2 out
of 6 in the Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 2 of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Cu202
b:49.1
occ:1.00
|
NE2
|
B:HIS162
|
2.0
|
45.3
|
1.0
|
ND1
|
B:HIS85
|
2.2
|
35.7
|
1.0
|
NE2
|
B:HIS104
|
2.4
|
33.9
|
1.0
|
O
|
B:HOH325
|
2.6
|
44.4
|
0.9
|
NE2
|
B:HIS87
|
2.7
|
37.5
|
1.0
|
CD2
|
B:HIS162
|
2.9
|
28.7
|
1.0
|
CG
|
B:HIS85
|
3.0
|
31.9
|
1.0
|
CE1
|
B:HIS162
|
3.0
|
31.2
|
1.0
|
CB
|
B:HIS85
|
3.1
|
28.0
|
1.0
|
CD2
|
B:HIS104
|
3.1
|
32.1
|
1.0
|
CE1
|
B:HIS85
|
3.3
|
37.1
|
1.0
|
CE1
|
B:HIS104
|
3.4
|
33.2
|
1.0
|
CD2
|
B:HIS87
|
3.5
|
39.5
|
1.0
|
CE1
|
B:HIS87
|
3.8
|
42.1
|
1.0
|
CG
|
B:HIS162
|
4.1
|
33.4
|
1.0
|
ND1
|
B:HIS162
|
4.1
|
38.9
|
1.0
|
O
|
B:HOH338
|
4.1
|
42.2
|
1.0
|
CD2
|
B:HIS85
|
4.2
|
31.5
|
1.0
|
CG
|
B:HIS104
|
4.3
|
32.2
|
1.0
|
NE2
|
B:HIS85
|
4.3
|
38.2
|
1.0
|
ND1
|
B:HIS104
|
4.3
|
22.2
|
1.0
|
CA
|
B:HIS85
|
4.4
|
30.8
|
1.0
|
CG1
|
B:VAL160
|
4.5
|
31.3
|
1.0
|
CB
|
B:VAL160
|
4.6
|
28.6
|
1.0
|
N
|
B:HIS85
|
4.7
|
25.5
|
1.0
|
CG
|
B:HIS87
|
4.7
|
41.0
|
1.0
|
ND1
|
B:HIS87
|
4.8
|
44.8
|
1.0
|
C
|
B:HIS85
|
5.0
|
30.3
|
1.0
|
O
|
B:ASN179
|
5.0
|
30.4
|
1.0
|
O
|
B:HIS85
|
5.0
|
28.9
|
1.0
|
|
Copper binding site 3 out
of 6 in 7ypr
Go back to
Copper Binding Sites List in 7ypr
Copper binding site 3 out
of 6 in the Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 3 of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Cu202
b:42.9
occ:1.00
|
NE2
|
C:HIS104
|
2.0
|
32.3
|
1.0
|
NE2
|
C:HIS162
|
2.0
|
37.6
|
1.0
|
ND1
|
C:HIS85
|
2.1
|
28.7
|
1.0
|
CD2
|
C:HIS162
|
2.9
|
32.0
|
1.0
|
CE1
|
C:HIS104
|
2.9
|
29.0
|
1.0
|
CG
|
C:HIS85
|
3.0
|
31.3
|
1.0
|
CD2
|
C:HIS104
|
3.0
|
29.9
|
1.0
|
O
|
C:HOH366
|
3.0
|
49.1
|
1.0
|
CE1
|
C:HIS85
|
3.1
|
34.9
|
1.0
|
CE1
|
C:HIS162
|
3.1
|
35.2
|
1.0
|
CB
|
C:HIS85
|
3.2
|
25.0
|
1.0
|
ND1
|
C:HIS104
|
4.0
|
23.8
|
1.0
|
CG
|
C:HIS162
|
4.0
|
30.6
|
1.0
|
CG
|
C:HIS104
|
4.1
|
33.2
|
1.0
|
ND1
|
C:HIS162
|
4.1
|
39.3
|
1.0
|
CD2
|
C:HIS85
|
4.1
|
33.5
|
1.0
|
NE2
|
C:HIS85
|
4.2
|
34.3
|
1.0
|
O
|
C:ASN179
|
4.4
|
32.2
|
1.0
|
O
|
C:HOH342
|
4.6
|
42.5
|
1.0
|
CB
|
C:ASN179
|
4.7
|
30.4
|
1.0
|
CA
|
C:HIS85
|
4.7
|
25.9
|
1.0
|
CG1
|
C:VAL160
|
4.9
|
31.8
|
1.0
|
|
Copper binding site 4 out
of 6 in 7ypr
Go back to
Copper Binding Sites List in 7ypr
Copper binding site 4 out
of 6 in the Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 4 of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Cu202
b:53.9
occ:1.00
|
NE2
|
D:HIS162
|
2.1
|
43.5
|
1.0
|
ND1
|
D:HIS85
|
2.1
|
47.7
|
1.0
|
NE2
|
D:HIS104
|
2.2
|
40.0
|
1.0
|
NE2
|
D:HIS87
|
2.7
|
61.4
|
1.0
|
CD2
|
D:HIS162
|
2.8
|
39.7
|
1.0
|
CG
|
D:HIS85
|
2.8
|
38.9
|
1.0
|
CB
|
D:HIS85
|
3.0
|
35.7
|
1.0
|
CD2
|
D:HIS104
|
3.1
|
34.7
|
1.0
|
CE1
|
D:HIS162
|
3.1
|
39.8
|
1.0
|
CE1
|
D:HIS85
|
3.1
|
45.3
|
1.0
|
CE1
|
D:HIS104
|
3.2
|
41.5
|
1.0
|
CE1
|
D:HIS87
|
3.5
|
45.9
|
1.0
|
CD2
|
D:HIS87
|
3.8
|
54.5
|
1.0
|
O
|
D:HOH304
|
3.9
|
30.0
|
1.0
|
CD2
|
D:HIS85
|
4.0
|
40.8
|
1.0
|
CG
|
D:HIS162
|
4.0
|
38.6
|
1.0
|
ND1
|
D:HIS162
|
4.1
|
41.2
|
1.0
|
NE2
|
D:HIS85
|
4.1
|
48.8
|
1.0
|
ND1
|
D:HIS104
|
4.2
|
27.5
|
1.0
|
CG
|
D:HIS104
|
4.2
|
37.5
|
1.0
|
CA
|
D:HIS85
|
4.5
|
38.7
|
1.0
|
ND1
|
D:HIS87
|
4.6
|
44.8
|
1.0
|
O
|
D:ASN179
|
4.8
|
43.2
|
1.0
|
CG
|
D:HIS87
|
4.8
|
48.9
|
1.0
|
N
|
D:HIS85
|
4.8
|
32.7
|
1.0
|
CG1
|
D:VAL160
|
5.0
|
35.1
|
1.0
|
|
Copper binding site 5 out
of 6 in 7ypr
Go back to
Copper Binding Sites List in 7ypr
Copper binding site 5 out
of 6 in the Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 5 of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Cu202
b:65.4
occ:1.00
|
NE2
|
E:HIS162
|
1.9
|
56.8
|
1.0
|
ND1
|
E:HIS85
|
2.1
|
53.7
|
1.0
|
CD2
|
E:HIS162
|
2.6
|
44.6
|
1.0
|
NE2
|
E:HIS104
|
2.7
|
62.0
|
1.0
|
NE2
|
E:HIS87
|
2.8
|
53.3
|
0.6
|
CG
|
E:HIS85
|
2.9
|
49.5
|
1.0
|
CE1
|
E:HIS162
|
3.1
|
55.1
|
1.0
|
O
|
E:HOH322
|
3.1
|
52.1
|
1.0
|
CE1
|
E:HIS85
|
3.1
|
50.4
|
1.0
|
CB
|
E:HIS85
|
3.2
|
49.6
|
1.0
|
CD2
|
E:HIS104
|
3.4
|
49.5
|
1.0
|
CD2
|
E:HIS87
|
3.6
|
50.9
|
0.6
|
CE1
|
E:HIS104
|
3.7
|
51.5
|
1.0
|
CE1
|
E:HIS87
|
3.8
|
55.5
|
0.6
|
CG
|
E:HIS162
|
3.8
|
51.3
|
1.0
|
ND1
|
E:HIS162
|
4.0
|
46.7
|
1.0
|
CD2
|
E:HIS85
|
4.1
|
53.1
|
1.0
|
NE2
|
E:HIS85
|
4.2
|
56.3
|
1.0
|
CG1
|
E:VAL160
|
4.3
|
48.1
|
1.0
|
CA
|
E:HIS85
|
4.5
|
49.8
|
1.0
|
CG
|
E:HIS104
|
4.6
|
52.5
|
1.0
|
CB
|
E:VAL160
|
4.6
|
49.6
|
1.0
|
N
|
E:HIS85
|
4.7
|
48.3
|
1.0
|
ND1
|
E:HIS104
|
4.7
|
45.5
|
1.0
|
CG
|
E:HIS87
|
4.8
|
51.2
|
0.6
|
ND1
|
E:HIS87
|
4.8
|
51.2
|
0.6
|
O
|
E:ASN179
|
5.0
|
51.5
|
1.0
|
|
Copper binding site 6 out
of 6 in 7ypr
Go back to
Copper Binding Sites List in 7ypr
Copper binding site 6 out
of 6 in the Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1.
Mono view
Stereo pair view
|
A full contact list of Copper with other atoms in the Cu binding
site number 6 of Structural Basis of A Superoxide Dismutase From A Tardigrade, Ramazzottius Varieornatus Strain Yokozuna-1. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Cu202
b:46.9
occ:0.77
|
NE2
|
F:HIS162
|
1.9
|
52.9
|
1.0
|
NE2
|
F:HIS104
|
2.0
|
48.9
|
1.0
|
ND1
|
F:HIS85
|
2.2
|
52.3
|
1.0
|
CE1
|
F:HIS162
|
2.8
|
53.5
|
1.0
|
CE1
|
F:HIS104
|
2.9
|
50.4
|
1.0
|
CD2
|
F:HIS162
|
2.9
|
47.9
|
1.0
|
CD2
|
F:HIS104
|
3.1
|
54.4
|
1.0
|
CG
|
F:HIS85
|
3.1
|
50.8
|
1.0
|
CE1
|
F:HIS85
|
3.2
|
50.2
|
1.0
|
O
|
F:HOH303
|
3.4
|
57.8
|
1.0
|
CB
|
F:HIS85
|
3.4
|
43.7
|
1.0
|
ND1
|
F:HIS162
|
3.9
|
46.9
|
1.0
|
CG
|
F:HIS162
|
3.9
|
50.0
|
1.0
|
ND1
|
F:HIS104
|
4.0
|
48.5
|
1.0
|
O
|
F:HOH326
|
4.1
|
55.9
|
1.0
|
CG
|
F:HIS104
|
4.1
|
41.3
|
1.0
|
CD2
|
F:HIS85
|
4.2
|
50.7
|
1.0
|
NE2
|
F:HIS85
|
4.2
|
52.9
|
1.0
|
O
|
F:ASN179
|
4.4
|
60.6
|
1.0
|
CB
|
F:ASN179
|
4.4
|
58.6
|
1.0
|
CA
|
F:HIS85
|
4.8
|
46.1
|
1.0
|
|
Reference:
K.S.Sim,
T.Inoue.
Structure of A Superoxide Dismutase From A Tardigrade: Ramazzottius Varieornatus Strain Yokozuna-1. Acta Crystallogr.,Sect.F V. 79 169 2023.
ISSN: ESSN 2053-230X
PubMed: 37358501
DOI: 10.1107/S2053230X2300523X
Page generated: Wed Jul 31 09:24:20 2024
|