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Copper in PDB 2zkw: Crystal Structure of Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21

Enzymatic activity of Crystal Structure of Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21

All present enzymatic activity of Crystal Structure of Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21, PDB code: 2zkw was solved by S.Yoshikawa, M.Kukimoto-Niino, K.Ito, L.Chen, Z.Q.Fu, J.Chrzas, B.C.Wang, M.Shirouzu, M.Urushitani, R.Takahashi, S.Yokoyama, Riken Structuralgenomics/Proteomics Initiative (Rsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.46 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 48.616, 46.233, 52.818, 90.00, 94.42, 90.00
R / Rfree (%) 19.3 / 25.2

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21 (pdb code 2zkw). 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 Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21, PDB code: 2zkw:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 2zkw

Go back to Copper Binding Sites List in 2zkw
Copper binding site 1 out of 2 in the Crystal Structure of Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21


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 Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu301

b:28.9
occ:1.00
ND1 A:HIS46 1.9 22.4 1.0
NE2 A:HIS48 2.0 28.2 1.0
NE2 A:HIS120 2.1 25.8 1.0
CE1 A:HIS46 2.9 19.4 1.0
CG A:HIS46 3.0 16.8 1.0
CD2 A:HIS48 3.0 33.7 1.0
CE1 A:HIS48 3.0 28.9 1.0
CD2 A:HIS120 3.1 32.5 1.0
CE1 A:HIS120 3.1 27.6 1.0
CB A:HIS46 3.3 26.6 1.0
NE2 A:HIS63 3.6 23.5 1.0
CD2 A:HIS63 3.7 29.0 1.0
CB A:VAL118 3.8 24.4 1.0
CG1 A:VAL118 4.0 26.8 1.0
NE2 A:HIS46 4.0 31.6 1.0
CD2 A:HIS46 4.1 21.7 1.0
ND1 A:HIS48 4.1 32.5 1.0
CG A:HIS48 4.1 29.1 1.0
N A:HIS46 4.1 27.9 1.0
ND1 A:HIS120 4.2 27.9 1.0
CG A:HIS120 4.2 26.8 1.0
CA A:HIS46 4.3 27.7 1.0
O A:VAL118 4.3 25.0 1.0
O A:HIS46 4.4 22.4 1.0
CE1 A:HIS63 4.5 30.1 1.0
CG2 A:VAL118 4.6 28.7 1.0
C A:HIS46 4.6 23.2 1.0
CG A:HIS63 4.8 27.7 1.0
C A:VAL118 4.8 28.1 1.0
CA A:VAL118 4.9 24.9 1.0
C A:PHE45 5.0 23.5 1.0

Copper binding site 2 out of 2 in 2zkw

Go back to Copper Binding Sites List in 2zkw
Copper binding site 2 out of 2 in the Crystal Structure of Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21


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 Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu302

b:26.1
occ:1.00
NE2 B:HIS48 1.9 18.7 1.0
ND1 B:HIS46 2.1 28.7 1.0
NE2 B:HIS120 2.1 26.8 1.0
CE1 B:HIS48 2.9 26.9 1.0
CD2 B:HIS48 3.0 22.2 1.0
CD2 B:HIS120 3.0 23.4 1.0
CG B:HIS46 3.0 30.5 1.0
CE1 B:HIS46 3.1 22.1 1.0
CE1 B:HIS120 3.2 22.4 1.0
CB B:HIS46 3.3 20.1 1.0
NE2 B:HIS63 3.5 24.1 1.0
CD2 B:HIS63 3.7 26.5 1.0
CB B:VAL118 3.9 25.5 1.0
ND1 B:HIS48 4.0 20.4 1.0
O B:HOH409 4.0 32.5 1.0
CG B:HIS48 4.1 32.7 1.0
CG1 B:VAL118 4.1 25.4 1.0
CG B:HIS120 4.2 25.4 1.0
NE2 B:HIS46 4.2 25.5 1.0
CD2 B:HIS46 4.2 27.9 1.0
ND1 B:HIS120 4.2 24.7 1.0
N B:HIS46 4.3 22.2 1.0
CA B:HIS46 4.3 19.7 1.0
O B:VAL118 4.3 19.4 1.0
CE1 B:HIS63 4.5 26.4 1.0
CG2 B:VAL118 4.7 28.8 1.0
O B:HIS46 4.7 23.9 1.0
C B:HIS46 4.7 21.6 1.0
CG B:HIS63 4.7 20.8 1.0
C B:VAL118 4.8 17.9 1.0
CA B:VAL118 4.9 25.9 1.0

Reference:

S.Yoshikawa, M.Kukimoto-Niino, K.Ito, L.Chen, Z.Q.Fu, J.Chrzas, B.C.Wang, M.Shirouzu, M.Urushitani, R.Takahashi, S.Yokoyama. Crystal Structure of Human Cu-Zn Superoxide Dismutase Mutant G85R in Space Group P21 To Be Published.
Page generated: Thu Sep 3 17:01:50 2020
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