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Copper in PDB 4oja: Structure of Hydra Cu-Zn Superoxide Dismutase

Enzymatic activity of Structure of Hydra Cu-Zn Superoxide Dismutase

All present enzymatic activity of Structure of Hydra Cu-Zn Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Structure of Hydra Cu-Zn Superoxide Dismutase, PDB code: 4oja was solved by A.Anupama, S.Ramaswamy, P.Sai Sudha, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.49 / 2.28
Space group P 64 2 2
Cell size a, b, c (Å), α, β, γ (°) 70.360, 70.360, 148.960, 90.00, 90.00, 120.00
R / Rfree (%) 19.1 / 24

Other elements in 4oja:

The structure of Structure of Hydra Cu-Zn Superoxide Dismutase also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Hydra Cu-Zn Superoxide Dismutase (pdb code 4oja). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Structure of Hydra Cu-Zn Superoxide Dismutase, PDB code: 4oja:

Copper binding site 1 out of 1 in 4oja

Go back to Copper Binding Sites List in 4oja
Copper binding site 1 out of 1 in the Structure of Hydra Cu-Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Hydra Cu-Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu201

b:25.5
occ:1.00
HD1 A:HIS45 1.6 17.3 1.0
NE2 A:HIS119 2.0 20.6 1.0
NE2 A:HIS47 2.2 18.7 1.0
HB2 A:HIS45 2.3 21.4 1.0
ND1 A:HIS45 2.4 14.2 1.0
NE2 A:HIS62 3.0 26.9 1.0
CE1 A:HIS119 3.0 12.5 1.0
CB A:HIS45 3.0 17.7 1.0
CE1 A:HIS47 3.0 14.4 1.0
CD2 A:HIS119 3.0 15.8 1.0
CG A:HIS45 3.0 15.0 1.0
HE1 A:HIS47 3.2 17.5 1.0
HE1 A:HIS119 3.2 15.2 1.0
CD2 A:HIS47 3.2 11.6 1.0
HD2 A:HIS119 3.2 19.2 1.0
HG13 A:VAL117 3.3 15.0 1.0
HD2 A:HIS62 3.3 32.5 1.0
HB A:VAL117 3.3 14.7 1.0
HB3 A:HIS45 3.4 21.4 1.0
HD2 A:HIS47 3.4 14.2 1.0
CD2 A:HIS62 3.4 26.9 1.0
CE1 A:HIS45 3.6 23.0 1.0
O A:HOH362 3.7 30.7 1.0
HE1 A:HIS45 3.9 27.8 1.0
CG1 A:VAL117 4.1 12.3 1.0
CE1 A:HIS62 4.1 22.7 1.0
CB A:VAL117 4.1 12.1 1.0
ND1 A:HIS119 4.1 18.4 1.0
CG A:HIS119 4.2 15.2 1.0
ND1 A:HIS47 4.2 18.0 1.0
CG A:HIS47 4.3 16.0 1.0
CA A:HIS45 4.3 13.7 1.0
CD2 A:HIS45 4.3 24.6 1.0
HE1 A:HIS62 4.4 27.5 1.0
H A:HIS45 4.5 18.4 1.0
O A:VAL117 4.5 19.9 1.0
NE2 A:HIS45 4.5 24.1 1.0
N A:HIS45 4.5 15.2 1.0
HG12 A:VAL117 4.6 15.0 1.0
CG A:HIS62 4.6 20.2 1.0
HG21 A:VAL117 4.7 13.4 1.0
HG11 A:VAL117 4.7 15.0 1.0
HG2 A:ARG142 4.7 18.3 1.0
O A:HIS45 4.7 12.8 1.0
C A:HIS45 4.8 12.9 1.0
ND1 A:HIS62 4.9 17.4 1.0
HD1 A:HIS119 4.9 22.3 1.0
HD1 A:HIS47 4.9 21.9 1.0
CG2 A:VAL117 5.0 11.0 1.0

Reference:

D.Subhadra, A.Anupama, J.Chirag, S.Ramaswamy, P.Sai Sudha. Structure of A Cu-Zn Superoxide Dismutase at An Evolutionary Crossroad. To Be Published.
Page generated: Sun Dec 13 11:15:27 2020

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