2P5N
Crystal structure of mouse 17-alpha hydroxysteroid dehydrogenase in complex with coenzyme NADPH
Summary for 2P5N
| Entry DOI | 10.2210/pdb2p5n/pdb |
| Descriptor | Aldo-keto reductase family 1, member C21, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total) |
| Functional Keywords | aldo-keto reductase, hydroxysteroid dehydrogenase, binary complex, tim barrel, oxidoreductase |
| Biological source | Mus musculus (house mouse) |
| Total number of polymer chains | 2 |
| Total formula weight | 75576.35 |
| Authors | El-Kabbani, O.,Dhagat, U. (deposition date: 2007-03-15, release date: 2007-10-09, Last modification date: 2024-11-13) |
| Primary citation | Dhagat, U.,Carbone, V.,Chung, R.P.,Schulze-Briese, C.,Endo, S.,Hara, A.,El-Kabbani, O. Structure of 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) holoenzyme from an orthorhombic crystal form: an insight into the bifunctionality of the enzyme. Acta Crystallogr.,Sect.F, 63:825-830, 2007 Cited by PubMed Abstract: Mouse 3(17)alpha-hydroxysteroid dehydrogenase (AKR1C21) is a bifunctional enzyme that catalyses the oxidoreduction of the 3- and 17-hydroxy/keto groups of steroid substrates such as oestrogens, androgens and neurosteroids. The structure of the AKR1C21-NADPH binary complex was determined from an orthorhombic crystal belonging to space group P2(1)2(1)2(1) at a resolution of 1.8 A. In order to identify the factors responsible for the bifunctionality of AKR1C21, three steroid substrates including a 17-keto steroid, a 3-keto steroid and a 3alpha-hydroxysteroid were docked into the substrate-binding cavity. Models of the enzyme-coenzyme-substrate complexes suggest that Lys31, Gly225 and Gly226 are important for ligand recognition and orientation in the active site. PubMed: 17909281DOI: 10.1107/S1744309107040985 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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