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1DT6

STRUCTURE OF MAMMALIAN CYTOCHROME P450 2C5

Summary for 1DT6
Entry DOI10.2210/pdb1dt6/pdb
DescriptorCYTOCHROME P450 2C5, SAMARIUM (III) ION, SULFATE ION, ... (4 entities in total)
Functional Keywordsmembrane protein, progesterone 21-hydroxylase, benzo(a)pyrene hydroxylase, estradiol 2-hydroxylase, p450, cyp2c5, oxidoreductase
Biological sourceOryctolagus cuniculus (rabbit)
Total number of polymer chains1
Total formula weight54939.29
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 citationWilliams, 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: 10678174
DOI: 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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