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Zinc in PDB 2jcw: Reduced Bridge-Broken Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure

Enzymatic activity of Reduced Bridge-Broken Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure

All present enzymatic activity of Reduced Bridge-Broken Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure:
1.15.1.1;

Protein crystallography data

The structure of Reduced Bridge-Broken Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 2jcw was solved by P.J.Hart, M.M.Balbirnie, N.L.Ogihara, A.M.Nersissian, M.S.Weiss, J.S.Valentine, D.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.70
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 119.280, 119.280, 75.050, 90.00, 90.00, 120.00
R / Rfree (%) 19.1 / n/a

Other elements in 2jcw:

The structure of Reduced Bridge-Broken Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure also contains other interesting chemical elements:

Copper (Cu) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Reduced Bridge-Broken Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure (pdb code 2jcw). 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 Reduced Bridge-Broken Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 2jcw:

Zinc binding site 1 out of 1 in 2jcw

Go back to Zinc Binding Sites List in 2jcw
Zinc binding site 1 out of 1 in the Reduced Bridge-Broken Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Reduced Bridge-Broken Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn155

b:18.9
occ:1.00
 OD1 A:ASP83 1.9 16.1 1.0
ND1 A:HIS63 2.0 16.3 1.0
ND1 A:HIS80 2.2 17.4 1.0
ND1 A:HIS71 2.2 15.6 1.0
CG A:ASP83 2.7 14.5 1.0
OD2 A:ASP83 2.9 16.5 1.0
CE1 A:HIS63 2.9 17.2 1.0
CG A:HIS63 3.1 15.7 1.0
CE1 A:HIS71 3.1 13.2 1.0
CE1 A:HIS80 3.1 16.1 1.0
CG A:HIS80 3.2 16.1 1.0
CG A:HIS71 3.3 14.3 1.0
CB A:HIS63 3.5 14.5 1.0
CB A:HIS80 3.6 14.8 1.0
CB A:HIS71 3.6 16.1 1.0
CA A:HIS71 3.9 17.2 1.0
O A:LYS136 4.0 21.3 1.0
NE2 A:HIS63 4.1 20.6 1.0
CB A:ASP83 4.2 16.0 1.0
CD2 A:HIS63 4.2 18.6 1.0
NE2 A:HIS80 4.2 18.3 1.0
NE2 A:HIS71 4.2 15.2 1.0
CD2 A:HIS80 4.3 16.1 1.0
CD2 A:HIS71 4.3 12.8 1.0
CA A:ASP83 4.7 18.0 1.0
N A:GLY72 4.8 16.8 1.0
N A:HIS80 4.8 17.4 1.0
CA A:HIS80 4.8 15.4 1.0
N A:ASP83 4.8 16.5 1.0
C A:HIS71 4.9 18.1 1.0
O A:HOH229 4.9 24.4 1.0
N A:HIS71 4.9 20.0 1.0
CD2 A:HIS46 4.9 15.4 1.0
CA A:HIS63 5.0 13.3 1.0
C A:LYS136 5.0 22.7 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: Thu Oct 17 01:12:13 2024

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