Arsenate reductase

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Revision as of 10:32, 7 January 2019

Structure of arsenate reductase complex with arsenate, thiarsahydroxy-cysteine, sulfate and Cs+ ion (dark purple) (PDB entry 1j9b)

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Updated on 07-January-2019

↑ 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

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 == Structural highlights ==
-The AsR active site contains a <scene name='54/547051/Cv/4'>catalytic Cys residue which forms a covalent thiolate-As V intermediate</scene>. <scene name='54/547051/Cv/3'>Entire active site</scene> (PDB entry [[1j9b]]).<ref>PMID:11709171</ref>
+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>