[Computer modeling of cytochrome P450 2E1 three-dimensional structure].
A computer model of human cytochrome P450 2E1 (CYP2E1) three-dimensional structure and active site was constructed based on homology with crystallographic coordinates of CYP2C5 and CYP2C9. A high degree of secondary structure homology for human, mouse, rat and rabbit CYP2E1 was demonstrated. The location of heme and the supporting alpha-helices was established. CYP2E1, CYP2C5 and CYP2C9 active sites are distinguished by pocket size and their amino acid residues composition. Key amino acid residues forming the active site channel and substrate-binding cavity are presented. Active site surface area and volume for CYP2E1, CYP2C5 and CYP2C9 were calculated.
Danko
I M
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Odynets
K A
KA
Kitam
V O
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Chashchin
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D000595:Amino Acid Sequence; D000818:Animals; D003198:Computer Simulation; D018360:Crystallography, X-Ray; D019392:Cytochrome P-450 CYP2E1 / Q000737:chemistry*; D006801:Humans; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D051381:Rats; D017386:Sequence Homology, Amino Acid
D019392:Cytochrome P-450 CYP2E1