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Zinc in PDB 1q0e: Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase

Enzymatic activity of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase

All present enzymatic activity of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase, PDB code: 1q0e was solved by M.A.Hough, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 46.953, 51.507, 148.410, 90.00, 90.00, 90.00
R / Rfree (%) 13.1 / 16.6

Other elements in 1q0e:

The structure of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase also contains other interesting chemical elements:

Copper (Cu) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase (pdb code 1q0e). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase, PDB code: 1q0e:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1q0e

Go back to Zinc Binding Sites List in 1q0e
Zinc binding site 1 out of 2 in the Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn153

b:12.6
occ:1.00
OD2 A:ASP81 2.0 12.9 1.0
ND1 A:HIS61 2.1 13.7 1.0
ND1 A:HIS69 2.1 13.6 1.0
ND1 A:HIS78 2.1 13.6 1.0
CG A:ASP81 2.7 12.5 1.0
OD1 A:ASP81 2.9 13.1 1.0
CE1 A:HIS69 2.9 15.5 1.0
CE1 A:HIS78 3.0 13.8 1.0
CE1 A:HIS61 3.0 14.3 1.0
CG A:HIS61 3.1 14.3 1.0
CG A:HIS78 3.1 12.3 1.0
CG A:HIS69 3.2 15.0 1.0
CB A:HIS61 3.5 14.6 1.0
CB A:HIS78 3.6 12.5 1.0
CB A:HIS69 3.7 14.8 1.0
CA A:HIS69 4.0 14.3 1.0
O A:LYS134 4.0 20.0 1.0
NE2 A:HIS78 4.1 14.2 1.0
NE2 A:HIS69 4.2 15.5 1.0
CB A:ASP81 4.2 12.7 1.0
NE2 A:HIS61 4.2 16.6 1.0
CD2 A:HIS78 4.2 13.4 1.0
CD2 A:HIS61 4.2 18.0 1.0
CD2 A:HIS69 4.3 16.7 1.0
CA A:ASP81 4.7 12.9 1.0
N A:HIS78 4.8 12.2 1.0
N A:GLY70 4.8 14.6 1.0
CA A:HIS78 4.9 12.2 1.0
O A:HOH3143 4.9 26.5 1.0
CD2 A:HIS44 5.0 14.3 1.0
C A:HIS69 5.0 14.7 1.0
N A:HIS69 5.0 15.7 1.0
C A:LYS134 5.0 19.5 1.0
N A:ASP81 5.0 12.0 1.0

Zinc binding site 2 out of 2 in 1q0e

Go back to Zinc Binding Sites List in 1q0e
Zinc binding site 2 out of 2 in the Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Atomic Resolution (1.15 ) Crystal Structure of Bovine Copper, Zinc Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn153

b:9.6
occ:1.00
OD2 B:ASP81 2.0 10.4 1.0
ND1 B:HIS61 2.1 10.2 1.0
ND1 B:HIS78 2.1 9.9 1.0
ND1 B:HIS69 2.1 10.8 1.0
CG B:ASP81 2.8 10.3 1.0
OD1 B:ASP81 2.9 11.0 1.0
CE1 B:HIS69 2.9 11.0 1.0
CE1 B:HIS78 3.0 10.9 1.0
CE1 B:HIS61 3.0 11.1 1.0
CG B:HIS61 3.1 10.7 1.0
CG B:HIS78 3.1 10.3 1.0
CG B:HIS69 3.2 10.3 1.0
CB B:HIS61 3.5 11.2 1.0
CB B:HIS78 3.6 10.5 1.0
CB B:HIS69 3.7 10.8 1.0
O B:LYS134 3.9 12.7 1.0
CA B:HIS69 4.0 10.6 1.0
NE2 B:HIS78 4.1 11.3 1.0
NE2 B:HIS69 4.1 10.7 1.0
CD2 B:HIS78 4.2 11.2 1.0
CD2 B:HIS61 4.2 12.6 1.0
NE2 B:HIS61 4.2 12.3 1.0
CB B:ASP81 4.2 10.6 1.0
CD2 B:HIS69 4.3 10.6 1.0
N B:HIS78 4.7 10.7 1.0
CA B:ASP81 4.8 10.4 1.0
N B:GLY70 4.8 10.8 1.0
CA B:HIS78 4.8 10.0 1.0
C B:LYS134 4.8 11.7 1.0
O B:HOH3023 4.9 14.6 1.0
CD2 B:HIS44 4.9 11.8 1.0
C B:HIS69 5.0 10.8 1.0
N B:ASP81 5.0 10.5 1.0

Reference:

M.A.Hough, S.S.Hasnain. Structure of Fully Reduced Bovine Copper Zinc Superoxide Dismutase at 1.15 A. Structure V. 11 937 2003.
ISSN: ISSN 0969-2126
PubMed: 12906825
DOI: 10.1016/S0969-2126(03)00155-2
Page generated: Wed Dec 16 03:01:23 2020

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