Zinc in PDB 3f7k: X-Ray Crystal Structure of An Alvinella Pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex

Enzymatic activity of X-Ray Crystal Structure of An Alvinella Pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex

All present enzymatic activity of X-Ray Crystal Structure of An Alvinella Pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex:
1.15.1.1;

Protein crystallography data

The structure of X-Ray Crystal Structure of An Alvinella Pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex, PDB code: 3f7k was solved by D.S.Shin, M.Didonato, D.P.Barondeau, E.D.Getzoff, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.00 / 1.35
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 62.563, 62.563, 163.745, 90.00, 90.00, 120.00
R / Rfree (%) 12.8 / 17.6

Other elements in 3f7k:

The structure of X-Ray Crystal Structure of An Alvinella Pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex also contains other interesting chemical elements:

Copper (Cu) 2 atoms
Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the X-Ray Crystal Structure of An Alvinella Pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex (pdb code 3f7k). 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 X-Ray Crystal Structure of An Alvinella Pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex, PDB code: 3f7k:

Zinc binding site 1 out of 1 in 3f7k

Go back to Zinc Binding Sites List in 3f7k
Zinc binding site 1 out of 1 in the X-Ray Crystal Structure of An Alvinella Pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Crystal Structure of An Alvinella Pompejana Cu,Zn Superoxide Dismutase- Hydrogen Peroxide Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn203

b:10.9
occ:1.00
 OD1 A:ASP81 2.0 11.2 1.0
ND1 A:HIS78 2.0 10.8 1.0
ND1 A:HIS61 2.0 11.7 1.0
ND1 A:HIS69 2.0 10.7 1.0
CG A:ASP81 2.7 11.3 1.0
CE1 A:HIS69 2.9 11.6 1.0
CE1 A:HIS78 2.9 11.1 1.0
OD2 A:ASP81 2.9 12.4 1.0
CE1 A:HIS61 2.9 12.9 1.0
CG A:HIS78 3.1 10.5 1.0
CG A:HIS61 3.1 13.2 1.0
CG A:HIS69 3.1 10.7 1.0
CB A:HIS61 3.4 12.4 1.0
CB A:HIS78 3.6 11.3 1.0
CB A:HIS69 3.7 11.7 1.0
CA A:HIS69 3.9 11.8 1.0
O A:ILE134 4.0 13.5 1.0
NE2 A:HIS78 4.1 12.5 1.0
NE2 A:HIS69 4.1 11.0 1.0
NE2 A:HIS61 4.1 13.0 1.0
CD2 A:HIS78 4.1 13.0 1.0
CD2 A:HIS61 4.2 13.7 1.0
CB A:ASP81 4.2 11.7 1.0
CD2 A:HIS69 4.2 11.9 1.0
CA A:ASP81 4.7 11.1 1.0
N A:HIS78 4.8 11.6 1.0
CD2 A:HIS44 4.8 12.4 1.0
CA A:HIS78 4.8 10.9 1.0
N A:GLY70 4.8 12.8 1.0
N A:HIS69 4.9 11.8 1.0
C A:HIS69 4.9 12.5 1.0
C A:ILE134 4.9 12.3 1.0
CA A:HIS61 4.9 11.0 1.0
N A:ASP81 5.0 11.3 1.0

Reference:

D.S.Shin, M.Didonato, D.P.Barondeau, G.L.Hura, C.Hitomi, J.A.Berglund, E.D.Getzoff, S.C.Cary, J.A.Tainer. Superoxide Dismutase From the Eukaryotic Thermophile Alvinella Pompejana: Structures, Stability, Mechanism, and Insights Into Amyotrophic Lateral Sclerosis. J.Mol.Biol. V. 385 1534 2009.
ISSN: ISSN 0022-2836
PubMed: 19063897
DOI: 10.1016/J.JMB.2008.11.031
Page generated: Thu Oct 24 13:05:15 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy