|
Atomistry » Arsenic » PDB 1q2o-1yhc » 1sk1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Arsenic » PDB 1q2o-1yhc » 1sk1 » |
Arsenic in PDB 1sk1: Arsenate Reductase R60K Mutant +0.4M Arsenate From E. ColiEnzymatic activity of Arsenate Reductase R60K Mutant +0.4M Arsenate From E. Coli
All present enzymatic activity of Arsenate Reductase R60K Mutant +0.4M Arsenate From E. Coli:
1.20.4.1; Protein crystallography data
The structure of Arsenate Reductase R60K Mutant +0.4M Arsenate From E. Coli, PDB code: 1sk1
was solved by
S.Demel,
B.F.Edwards,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1sk1:
The structure of Arsenate Reductase R60K Mutant +0.4M Arsenate From E. Coli also contains other interesting chemical elements:
Arsenic Binding Sites:
The binding sites of Arsenic atom in the Arsenate Reductase R60K Mutant +0.4M Arsenate From E. Coli
(pdb code 1sk1). This binding sites where shown within
5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Arsenate Reductase R60K Mutant +0.4M Arsenate From E. Coli, PDB code: 1sk1: Arsenic binding site 1 out of 1 in 1sk1Go back to Arsenic Binding Sites List in 1sk1
Arsenic binding site 1 out
of 1 in the Arsenate Reductase R60K Mutant +0.4M Arsenate From E. Coli
Mono view Stereo pair view
Reference:
S.Demel,
J.Shi,
P.Martin,
B.P.Rosen,
B.F.Edwards.
Arginine 60 in the Arsc Arsenate Reductase of E. Coli Plasmid R773 Determines the Chemical Nature of the Bound As(III) Product. Protein Sci. V. 13 2330 2004.
Page generated: Wed Jul 10 11:13:26 2024
ISSN: ISSN 0961-8368 PubMed: 15295115 DOI: 10.1110/PS.04787204 |
Last articlesZn in 9JYWZn in 9IR4 Zn in 9IR3 Zn in 9GMX Zn in 9GMW Zn in 9JEJ Zn in 9ERF Zn in 9ERE Zn in 9EGV Zn in 9EGW |
© Copyright 2008-2020 by atomistry.com | ||
Home | Site Map | Copyright | Contact us | Privacy |