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Atomistry » Arsenic » PDB 1z6b-2im2 » 2acr » |
Arsenic in PDB 2acr: An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- PhosphateEnzymatic activity of An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate
All present enzymatic activity of An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate:
1.1.1.21; Protein crystallography data
The structure of An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate, PDB code: 2acr
was solved by
D.H.Harrison,
K.M.Bohren,
K.H.Gabbay,
G.A.Petsko,
D.Ringe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Arsenic Binding Sites:
The binding sites of Arsenic atom in the An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate
(pdb code 2acr). 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 An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate, PDB code: 2acr: Arsenic binding site 1 out of 1 in 2acrGo back to Arsenic Binding Sites List in 2acr
Arsenic binding site 1 out
of 1 in the An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose-6- Phosphate
Mono view Stereo pair view
Reference:
D.H.Harrison,
K.M.Bohren,
D.Ringe,
G.A.Petsko,
K.H.Gabbay.
An Anion Binding Site in Human Aldose Reductase: Mechanistic Implications For the Binding of Citrate, Cacodylate, and Glucose 6-Phosphate. Biochemistry V. 33 2011 1994.
Page generated: Sat Dec 12 01:37:46 2020
ISSN: ISSN 0006-2960 PubMed: 8117658 DOI: 10.1021/BI00174A006 |
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