3C3U
Crystal structure of AKR1C1 in complex with NADP and 3,5-dichlorosalicylic acid
Summary for 3C3U
| Entry DOI | 10.2210/pdb3c3u/pdb |
| Descriptor | Aldo-keto reductase family 1 member C1, ZINC ION, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | aldo-keto reductase, 20 alpha hydroxysteroid dehydrogenase, akr1c1, cytoplasm, nadp, oxidoreductase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasm: Q04828 |
| Total number of polymer chains | 1 |
| Total formula weight | 37855.16 |
| Authors | Dhagat, U.,El-Kabbani, O. (deposition date: 2008-01-28, release date: 2008-08-26, Last modification date: 2023-11-01) |
| Primary citation | Dhagat, U.,Endo, S.,Sumii, R.,Hara, A.,El-Kabbani, O. Selectivity determinants of inhibitor binding to human 20alpha-hydroxysteroid dehydrogenase: crystal structure of the enzyme in ternary complex with coenzyme and the potent inhibitor 3,5-dichlorosalicylic acid J.Med.Chem., 51:4844-4848, 2008 Cited by PubMed Abstract: The crystal structure of human 20alpha-hydroxysteroid dehydrogenase (AKR1C1) in ternary complex with the coenzyme NADP (+) and the potent inhibitor 3,5-dichlorosalicylic acid was determined at a resolution of 1.8 A. The inhibitor is held in place by a network of hydrogen bonding interactions with the active site residues Tyr55, His117, and His222. The important role of the nonconserved residues Leu54, His222, Leu306, and Leu308 in inhibitor binding and selectivity was determined by site-directed mutagenesis. PubMed: 18620380DOI: 10.1021/jm8003575 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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