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Zinc 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:

Copper (Cu) 1 atom

Zinc Binding Sites:

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

Zinc binding site 1 out of 1 in 4oja

Go back to Zinc Binding Sites List in 4oja
Zinc 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 Zinc with other atoms in the Zn binding site number 1 of Structure of Hydra Cu-Zn Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn202

b:20.3
occ:1.00
HD1 A:HIS62 1.4 21.1 1.0
HD1 A:HIS70 1.4 27.8 1.0
OD1 A:ASP82 2.0 18.7 1.0
ND1 A:HIS79 2.0 25.7 1.0
ND1 A:HIS70 2.2 23.0 1.0
ND1 A:HIS62 2.2 17.4 1.0
CG A:ASP82 2.7 18.1 1.0
OD2 A:ASP82 2.7 19.0 1.0
CE1 A:HIS79 2.9 24.5 1.0
CE1 A:HIS70 2.9 19.3 1.0
HB2 A:HIS79 2.9 27.4 1.0
HE1 A:HIS70 3.0 23.3 1.0
HE1 A:HIS79 3.0 29.6 1.0
CG A:HIS79 3.1 27.3 1.0
HA A:HIS70 3.1 29.2 1.0
CG A:HIS62 3.2 20.2 1.0
CE1 A:HIS62 3.2 22.7 1.0
HB2 A:HIS62 3.2 18.1 1.0
CG A:HIS70 3.2 30.7 1.0
HB3 A:HIS62 3.2 18.1 1.0
HE1 A:HIS62 3.4 27.5 1.0
CB A:HIS62 3.4 14.9 1.0
HB2 A:HIS70 3.5 25.9 1.0
CB A:HIS79 3.5 22.7 1.0
CB A:HIS70 3.7 21.4 1.0
O A:THR135 3.8 33.0 1.0
CA A:HIS70 3.9 24.2 1.0
H A:HIS79 4.0 31.8 1.0
NE2 A:HIS79 4.0 19.5 1.0
HB3 A:HIS79 4.0 27.4 1.0
NE2 A:HIS70 4.0 25.0 1.0
CD2 A:HIS79 4.1 20.3 1.0
H A:GLY71 4.1 23.1 1.0
CB A:ASP82 4.1 15.1 1.0
CD2 A:HIS70 4.2 28.6 1.0
CD2 A:HIS62 4.3 26.9 1.0
NE2 A:HIS62 4.3 26.9 1.0
HA A:ASP82 4.3 26.2 1.0
HA A:THR136 4.5 32.2 1.0
HB3 A:ASP82 4.5 18.3 1.0
N A:HIS79 4.7 26.3 1.0
HB3 A:HIS70 4.7 25.9 1.0
CA A:HIS79 4.7 19.1 1.0
CA A:ASP82 4.7 21.6 1.0
N A:GLY71 4.7 19.1 1.0
HB2 A:ASP82 4.7 18.3 1.0
O A:HOH339 4.7 21.6 1.0
HE2 A:HIS79 4.8 23.7 1.0
HE2 A:HIS70 4.8 30.2 1.0
C A:THR135 4.8 30.5 1.0
C A:HIS70 4.8 19.7 1.0
N A:ASP82 4.9 21.2 1.0
N A:HIS70 4.9 26.1 1.0
H A:ASP82 4.9 25.6 1.0
HD2 A:HIS79 5.0 24.6 1.0
CA A:HIS62 5.0 19.3 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: Wed Aug 20 21:05:31 2025

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