1I9D
ARSENATE REDUCTASE FROM E. COLI
Summary for 1I9D
Entry DOI | 10.2210/pdb1i9d/pdb |
Descriptor | ARSENATE REDUCTASE, SULFATE ION, SULFITE ION, ... (5 entities in total) |
Functional Keywords | arsenic, arsenate, reductase, oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 17546.54 |
Authors | Martin, P.,Edwards, B.F. (deposition date: 2001-03-19, release date: 2001-12-05, Last modification date: 2024-02-07) |
Primary citation | Martin, P.,DeMel, S.,Shi, J.,Gladysheva, T.,Gatti, D.L.,Rosen, B.P.,Edwards, B.F. Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. Structure, 9:1071-1081, 2001 Cited by PubMed Abstract: In Escherichia coli bearing the plasmid R773, resistance to arsenite, arsenate, antimonite, and tellurite is conferred by the arsRDABC plasmid operon that codes for an ATP-dependent anion pump. The product of the arsC gene, arsenate reductase (ArsC), is required to efficiently catalyze the reduction of arsenate to arsenite prior to extrusion. PubMed: 11709171DOI: 10.1016/S0969-2126(01)00672-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.65 Å) |
Structure validation
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