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Zinc in PDB 1yaz: Azide-Bound Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure

Enzymatic activity of Azide-Bound Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure

All present enzymatic activity of Azide-Bound Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure:
1.15.1.1;

Protein crystallography data

The structure of Azide-Bound Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 1yaz 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) 90.00 / 1.70
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 119.375, 119.375, 74.543, 90.00, 90.00, 120.00
R / Rfree (%) 16.9 / 20.8

Other elements in 1yaz:

The structure of Azide-Bound Yeast Cu(II)/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 Azide-Bound Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure (pdb code 1yaz). 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 Azide-Bound Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 1yaz:

Zinc binding site 1 out of 1 in 1yaz

Go back to Zinc Binding Sites List in 1yaz
Zinc binding site 1 out of 1 in the Azide-Bound Yeast Cu(II)/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 Azide-Bound Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn155

b:20.1
occ:1.00
 OD1 A:ASP83 1.9 17.9 1.0
ND1 A:HIS63 2.0 21.0 1.0
ND1 A:HIS71 2.0 18.8 1.0
ND1 A:HIS80 2.2 21.4 1.0
CG A:ASP83 2.8 26.5 1.0
CE1 A:HIS71 2.9 20.7 1.0
OD2 A:ASP83 2.9 22.2 1.0
CE1 A:HIS63 2.9 21.0 1.0
CG A:HIS63 3.0 20.8 1.0
CE1 A:HIS80 3.1 19.9 1.0
CG A:HIS80 3.1 19.5 1.0
CG A:HIS71 3.2 21.1 1.0
CB A:HIS63 3.5 16.6 1.0
CB A:HIS80 3.5 19.1 1.0
CB A:HIS71 3.7 22.4 1.0
O A:LYS136 3.9 26.4 1.0
CA A:HIS71 4.0 22.4 1.0
NE2 A:HIS63 4.1 22.8 1.0
NE2 A:HIS71 4.1 20.9 1.0
CD2 A:HIS63 4.2 20.1 1.0
NE2 A:HIS80 4.2 20.5 1.0
CB A:ASP83 4.2 22.0 1.0
CD2 A:HIS80 4.2 19.3 1.0
CD2 A:HIS71 4.2 20.4 1.0
CA A:ASP83 4.6 19.5 1.0
N A:GLY72 4.8 21.7 1.0
N A:HIS80 4.8 20.0 1.0
C A:LYS136 4.8 25.6 1.0
CA A:HIS80 4.8 17.4 1.0
N A:ASP83 4.8 17.3 1.0
C A:HIS71 4.9 23.2 1.0
O A:HOH168 4.9 30.6 1.0
N A:HIS71 4.9 22.3 1.0
CA A:THR137 5.0 24.9 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: Wed Oct 16 20:49:12 2024

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