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Atomistry » Caesium » PDB 1av2-2j9x » 1s3c | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Caesium » PDB 1av2-2j9x » 1s3c » |
Caesium in PDB 1s3c: Arsenate Reductase C12S Mutant From E. ColiEnzymatic activity of Arsenate Reductase C12S Mutant From E. Coli
All present enzymatic activity of Arsenate Reductase C12S Mutant From E. Coli:
1.20.4.1; Protein crystallography data
The structure of Arsenate Reductase C12S Mutant From E. Coli, PDB code: 1s3c
was solved by
S.Demel,
B.F.Edwards,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Caesium Binding Sites:
The binding sites of Caesium atom in the Arsenate Reductase C12S Mutant From E. Coli
(pdb code 1s3c). This binding sites where shown within
5.0 Angstroms radius around Caesium atom.
In total 3 binding sites of Caesium where determined in the Arsenate Reductase C12S Mutant From E. Coli, PDB code: 1s3c: Jump to Caesium binding site number: 1; 2; 3; Caesium binding site 1 out of 3 in 1s3cGo back to Caesium Binding Sites List in 1s3c
Caesium binding site 1 out
of 3 in the Arsenate Reductase C12S Mutant From E. Coli
Mono view Stereo pair view
Caesium binding site 2 out of 3 in 1s3cGo back to Caesium Binding Sites List in 1s3c
Caesium binding site 2 out
of 3 in the Arsenate Reductase C12S Mutant From E. Coli
Mono view Stereo pair view
Caesium binding site 3 out of 3 in 1s3cGo back to Caesium Binding Sites List in 1s3c
Caesium binding site 3 out
of 3 in the Arsenate Reductase C12S Mutant 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: Sun Dec 13 10:55:33 2020
ISSN: ISSN 0961-8368 PubMed: 15295115 DOI: 10.1110/PS.04787204 |
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