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Zinc in PDB 1f18: Crystal Structure of Yeast Copper-Zinc Superoxide Dismutase Mutant GLY85ARG

Enzymatic activity of Crystal Structure of Yeast Copper-Zinc Superoxide Dismutase Mutant GLY85ARG

All present enzymatic activity of Crystal Structure of Yeast Copper-Zinc Superoxide Dismutase Mutant GLY85ARG:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of Yeast Copper-Zinc Superoxide Dismutase Mutant GLY85ARG, PDB code: 1f18 was solved by P.J.Hart, N.L.Ogihara, H.Liu, A.M.Nersissian, J.S.Valentine, D.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.00 / 1.70
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 118.500, 118.500, 73.400, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 23.4

Other elements in 1f18:

The structure of Crystal Structure of Yeast Copper-Zinc Superoxide Dismutase Mutant GLY85ARG also contains other interesting chemical elements:

Copper (Cu) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Yeast Copper-Zinc Superoxide Dismutase Mutant GLY85ARG (pdb code 1f18). 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 Crystal Structure of Yeast Copper-Zinc Superoxide Dismutase Mutant GLY85ARG, PDB code: 1f18:

Zinc binding site 1 out of 1 in 1f18

Go back to Zinc Binding Sites List in 1f18
Zinc binding site 1 out of 1 in the Crystal Structure of Yeast Copper-Zinc Superoxide Dismutase Mutant GLY85ARG


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Yeast Copper-Zinc Superoxide Dismutase Mutant GLY85ARG within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn155

b:14.8
occ:1.00
 ND1 A:HIS71 2.0 13.4 1.0
ND1 A:HIS63 2.0 18.6 1.0
OD1 A:ASP83 2.1 21.2 1.0
ND1 A:HIS80 2.2 21.4 1.0
CE1 A:HIS71 2.8 14.3 1.0
CE1 A:HIS63 2.9 18.7 1.0
CG A:ASP83 2.9 17.9 1.0
OD2 A:ASP83 3.0 16.8 1.0
CG A:HIS63 3.1 18.1 1.0
CE1 A:HIS80 3.1 21.3 1.0
CG A:HIS71 3.2 13.1 1.0
CG A:HIS80 3.2 20.2 1.0
CB A:HIS63 3.5 15.7 1.0
CB A:HIS80 3.6 17.3 1.0
CB A:HIS71 3.7 14.1 1.0
CA A:HIS71 4.0 17.3 1.0
NE2 A:HIS71 4.0 16.2 1.0
NE2 A:HIS63 4.0 21.3 1.0
O A:LYS136 4.1 18.8 1.0
CD2 A:HIS63 4.1 17.0 1.0
CD2 A:HIS71 4.2 12.7 1.0
NE2 A:HIS80 4.2 20.6 1.0
CD2 A:HIS80 4.3 18.7 1.0
CB A:ASP83 4.3 16.7 1.0
CA A:ASP83 4.7 18.1 1.0
CD2 A:HIS46 4.8 15.0 1.0
N A:HIS80 4.8 17.9 1.0
CA A:HIS80 4.8 17.1 1.0
N A:ASP83 4.9 15.3 1.0
O A:HOH230 4.9 18.1 1.0
N A:GLY72 4.9 17.2 1.0
C A:LYS136 4.9 18.8 1.0
C A:HIS71 5.0 16.0 1.0
N A:HIS71 5.0 19.0 1.0

Reference:

P.J.Hart, M.M.Balbirnie, N.L.Ogihara, A.M.Nersissian, M.S.Weiss, J.S.Valentine, D.Eisenberg. A Structure-Based Mechanism For Copper-Zinc Superoxide Dismutase. Biochemistry V. 38 2167 1999.
ISSN: ISSN 0006-2960
PubMed: 10026301
DOI: 10.1021/BI982284U
Page generated: Sun Oct 13 00:36:02 2024

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