Arsenate reductase: Difference between revisions
Jump to navigation
Jump to search
Michal Harel (talk | contribs) No edit summary |
No edit summary |
||
Line 11: | Line 11: | ||
== 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 16:17, 8 December 2015
|
3D structures of arsenate reducatse3D structures of arsenate reducatse
Updated on 08-December-2015
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