Arsenate reductase
From Proteopedia
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== Structural highlights == | == 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>. | + | 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> |
</StructureSection> | </StructureSection> | ||
Revision as of 13:17, 8 December 2015
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3D structures of arsenate reducatse
Updated on 08-December-2015
References
- ↑ 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
