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Ligands
Code Name Style Show Link
SM Samarium (III) ion
SO4 Sulfate ion
HEM Protoporphyrin ix containing Fe
Non-standard Residues
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Glycosylation
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Code : 1DT6   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : STRUCTURE OF MAMMALIAN CYTOCHROME P450 2C5
Release Data : 2000-09-27
Compound :
mol_id molecule chains synonym
1 CYTOCHROME P450 2C5 A PROGESTERONE 21-HYDROXYLASE, CYPIIC5 P450 1, P450IIC5
ec: 1.14.14.1
fragment: CYP2C5 WITH MEMBRANE SPANNING RESIDUES 3-21 DELETED AND A 4 RESIDUE HISTIDINE TAG AT THE C-TERMINUS CONTAINING ADDITIONAL INTERNAL MUTATIONS
mutation: D2A, H24S, G25S, N202H, R206E, I207L, S209G, S210T
Source :
mol_id organism_scientific organism_common expression_system
1 Oryctolagus cuniculus  (taxid:9986) Rabbit Escherichia coli  (taxid:562)
tissue: LIVER
expression_system_vector_type: PLASMID
expression_system_plasmid: PCW
Authors : Williams, P.A., Cosme, J., Sridhar, V., Johnson, E.F., McRee, D.E.
Keywords : membrane protein, progesterone 21-hydroxylase, benzo(a)pyrene hydroxylase, estradiol 2-hydroxylase, P450, CYP2C5, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 3.0 Å )
Citation :

Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity.

Williams, P.A.,Cosme, J.,Sridhar, V.  et al.
(2000)  Mol.Cell  5 : 121 - 131

PubMed: 10678174
DOI: 10.1016/S1097-2765(00)80408-6

Engineering Microsomal Cytochrome P450 2C5 to be a Soluble, Monomeric Enzyme. Mutations that Alter Aggregation, Phospholipid Dependence of Catalysis and Membrane Binding

Cosme, J.,Johnson, E.F.
(2000)  J.Biol.Chem.  275 : 2545 - 2553

DOI: 10.1074/jbc.275.4.2545

Chain : A
UniProt : P00179 (CP2C5_RABIT)
Reaction: EC: Evidence:
Physiological Direction:
an organic molecule + reduced [NADPH--hemoprotein reductase] + O2 = an alcohol + oxidized [NADPH--hemoprotein reductase] + H2O + H(+) 1.14.14.1 -
-
Cofactor: Evidence: Note:
heme - -