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Copper in PDB 2vr6: Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution

Enzymatic activity of Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution

All present enzymatic activity of Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution, PDB code: 2vr6 was solved by S.Antonyuk, X.Cao, S.V.Seetharaman, L.J.Whitson, A.B.Taylor, S.P.Holloway, R.W.Strange, P.A.Doucette, A.Tiwari, L.J.Hayward, S.Padua, J.A.Cohlberg, J.Selverstone Valentine, S.S.Hasnain, P.J.Hart, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.3
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 35.296, 73.746, 111.424, 90.00, 90.00, 90.00
R / Rfree (%) 13.2 / 18.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution (pdb code 2vr6). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution, PDB code: 2vr6:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2vr6

Go back to Copper Binding Sites List in 2vr6
Copper binding site 1 out of 2 in the Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1154

b:13.1
occ:0.20
ZN A:ZN1155 1.0 8.0 0.8
ND1 A:HIS46 1.6 9.3 1.0
NE2 A:HIS48 2.2 8.1 1.0
NE2 A:HIS120 2.2 8.7 1.0
CG A:HIS46 2.4 8.8 1.0
CB A:HIS46 2.7 8.3 1.0
CE1 A:HIS46 2.8 10.8 1.0
O1 A:SO41157 2.9 7.7 0.8
CD2 A:HIS120 2.9 7.3 1.0
CD2 A:HIS48 3.0 9.9 1.0
CE1 A:HIS48 3.3 9.4 1.0
CE1 A:HIS120 3.3 9.6 1.0
CD2 A:HIS46 3.6 8.9 1.0
NE2 A:HIS46 3.8 9.3 1.0
NE2 A:HIS63 3.9 9.6 1.0
CA A:HIS46 4.0 7.9 1.0
CD2 A:HIS63 4.1 11.0 1.0
CG A:HIS120 4.1 9.4 1.0
CB A:VAL118 4.2 7.9 1.0
S A:SO41157 4.2 9.3 0.8
N A:HIS46 4.2 7.3 1.0
CG A:HIS48 4.3 8.3 1.0
ND1 A:HIS120 4.3 9.8 1.0
ND1 A:HIS48 4.4 9.3 1.0
CG1 A:VAL118 4.4 10.2 1.0
O2 A:SO41157 4.5 8.5 0.8
CE1 A:HIS63 4.6 9.3 1.0
C A:HIS46 4.7 7.7 1.0
O A:VAL118 4.7 8.4 1.0
O A:HIS46 4.7 8.0 1.0
CG2 A:VAL118 4.9 9.0 1.0
O4 A:SO41157 5.0 12.4 0.8

Copper binding site 2 out of 2 in 2vr6

Go back to Copper Binding Sites List in 2vr6
Copper binding site 2 out of 2 in the Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Cu1155

b:7.2
occ:0.20
ZN F:ZN1154 1.3 7.9 0.8
ND1 F:HIS46 1.8 10.4 1.0
NE2 F:HIS48 2.3 8.7 1.0
NE2 F:HIS120 2.3 9.2 1.0
CG F:HIS46 2.4 9.2 1.0
CB F:HIS46 2.5 9.3 1.0
CD2 F:HIS120 2.9 8.0 1.0
CD2 F:HIS48 2.9 9.1 1.0
CE1 F:HIS46 3.0 10.8 1.0
O1 F:SO41157 3.3 8.0 0.8
CE1 F:HIS48 3.4 9.4 1.0
CE1 F:HIS120 3.5 9.2 1.0
CD2 F:HIS46 3.7 9.2 1.0
CA F:HIS46 3.8 7.7 1.0
CB F:VAL118 3.9 7.0 1.0
NE2 F:HIS46 3.9 9.0 1.0
N F:HIS46 4.0 7.9 1.0
CG1 F:VAL118 4.0 8.6 1.0
NE2 F:HIS63 4.1 11.0 1.0
CG F:HIS120 4.2 8.3 1.0
CG F:HIS48 4.2 8.1 1.0
CD2 F:HIS63 4.4 11.2 1.0
ND1 F:HIS48 4.4 8.7 1.0
O F:VAL118 4.4 8.1 1.0
ND1 F:HIS120 4.4 8.5 1.0
O F:HIS46 4.4 6.4 1.0
C F:HIS46 4.4 6.4 1.0
S F:SO41157 4.6 9.2 0.8
CG2 F:VAL118 4.6 7.8 1.0
O2 F:SO41157 4.7 9.2 0.8
CE1 F:HIS63 4.8 8.4 1.0
C F:PHE45 4.9 8.1 1.0
C F:VAL118 4.9 7.9 1.0
CA F:VAL118 4.9 7.0 1.0

Reference:

X.Cao, S.Antonyuk, S.V.Seetharaman, L.J.Whitson, A.B.Taylor, S.P.Holloway, R.W.Strange, P.A.Doucette, J.S.Valentine, A.Tiwari, L.J.Hayward, S.Padua, J.A.Cohlberg, S.S.Hasnain, P.J.Hart. Structures of the G85R Variant of SOD1 in Familial Amyotrophic Lateral Sclerosis. J.Biol.Chem. V. 283 16169 2008.
ISSN: ISSN 0021-9258
PubMed: 18378676
DOI: 10.1074/JBC.M801522200
Page generated: Thu Sep 3 16:51:50 2020
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