1DT6
STRUCTURE OF MAMMALIAN CYTOCHROME P450 2C5
Summary for 1DT6
| Entry DOI | 10.2210/pdb1dt6/pdb |
| Descriptor | CYTOCHROME P450 2C5, SAMARIUM (III) ION, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | membrane protein, progesterone 21-hydroxylase, benzo(a)pyrene hydroxylase, estradiol 2-hydroxylase, p450, cyp2c5, oxidoreductase |
| Biological source | Oryctolagus cuniculus (rabbit) |
| Total number of polymer chains | 1 |
| Total formula weight | 54939.29 |
| Authors | Williams, P.A.,Cosme, J.,Sridhar, V.,Johnson, E.F.,McRee, D.E. (deposition date: 2000-01-11, release date: 2000-09-27, Last modification date: 2024-10-30) |
| Primary citation | Williams, P.A.,Cosme, J.,Sridhar, V.,Johnson, E.F.,McRee, D.E. Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity. Mol.Cell, 5:121-131, 2000 Cited by PubMed Abstract: Microsomal cytochrome P450s participate in xenobiotic detoxification, procarcinogen activation, and steroid hormone synthesis. The first structure of a mammalian microsomal P450 suggests that the association of P450s with the endoplasmic reticulum involves a hydrophobic surface of the protein formed by noncontiguous portions of the polypeptide chain. This interaction places the entrance of the putative substrate access channel in or near the membrane and orients the face of the protein proximal to the heme cofactor perpendicular to the plane of the membrane for interaction with the P450 reductase. This structure offers a template for modeling other mammalian P450s and should aid drug discovery and the prediction of drug-drug interactions. PubMed: 10678174DOI: 10.1016/S1097-2765(00)80408-6 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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