Arsenate reductase: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The AsR active site contains a <scene name='54/547051/Cv/ | The AsR active site contains a <scene name='54/547051/Cv/5'>catalytic Cys residue which forms a covalent thiolate-As V intermediate</scene>. <scene name='54/547051/Cv/6'>Entire active site</scene> (PDB entry [[1j9b]]).<ref>PMID:11709171</ref> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:32, 7 January 2019
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3D structures of arsenate reductase3D structures of arsenate reductase
Updated on 07-January-2019
ReferencesReferences
- ↑ Holmgren A, Aslund F. Glutaredoxin. Methods Enzymol. 1995;252:283-92. PMID:7476363
- ↑ Martin P, DeMel S, Shi J, Gladysheva T, Gatti DL, Rosen BP, Edwards BF. Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. Structure. 2001 Nov;9(11):1071-81. PMID:11709171