Copper in PDB 2vr6: 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;

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

The structure of Crystal Structure of G85R Als Mutant of Human Cu,Zn Superoxide Dismutase (Cuznsod) at 1.3 A Resolution also contains other interesting chemical elements:

Zinc

(Zn)

4 atoms

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 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 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

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