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Ligands
Code Name Style Show Link
HEM Protoporphyrin ix containing Fe
TMI 1-[phenyl-(4-phenylphenyl)-methyl]imidazole
CM5 5-cyclohexyl-1-pentyl-beta-D-maltoside
Non-standard Residues
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Code : 2BDM   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Structure of Cytochrome P450 2B4 with Bound Bifonazole
Release Data : 2005-12-27
Compound :
mol_id molecule chains synonym
1 Cytochrome P450 2B4 A CYPIIB4, P450-LM2, Isozyme 2, P450 types B0 and B1
ec: 1.14.14.1
fragment: residues 28-491
Source :
mol_id organism_scientific organism_common expression_system
1 Oryctolagus cuniculus  (taxid:9986) Rabbit Escherichia coli  (taxid:562)
gene: CYP2B4
expression_system_strain: TOPP3
expression_system_vector_type: plasmid
expression_system_plasmid: pKK
Authors : Zhao, Y., White, M.A., Muralidhara, B.K., Sun, L., Halpert, J.R., Stout, C.D.
Keywords : p450, Monooxygenase, Oxidoreductase, membrane protein, CYP 2B4, CYP LM2
Exp. method : X-RAY DIFFRACTION ( 2.300 Å )
Citation :

Structure of microsomal cytochrome P450 2B4 complexed with the antifungal drug bifonazole: insight into P450 conformational plasticity and membrane interaction.

Zhao, Y.,White, M.A.,Muralidhara, B.K.  et al.
(2006)  J.Biol.Chem.  281 : 5973 - 5981

PubMed: 16373351
DOI: 10.1074/jbc.M511464200

An open conformation of mammalian cytochrome P450 2B4 at 1.6-resolution

Scott, E.E.,He, Y.A.,Wester, M.R.  et al.
(2003)  Proc.Natl.Acad.Sci.USA  100 : 13196 - 13201

PubMed: 14563924
DOI: 10.1073/pnas.2133986100

Structure of mammalian cytochrome P450 2B4 complexed with 4-(4-chlorophenyl)imidazole at 1.9-A resolution: insight into the range of P450 conformations and the coordination of redox partner binding

Scott, E.E.,White, M.A.,He, Y.A.  et al.
(2004)  J.Biol.Chem.  279 : 27294 - 27301

PubMed: 15100217
DOI: 10.1074/jbc.M403349200

Chain : A
UniProt : P00178 (CP2B4_RABIT)
Reaction: EC: Evidence:
Physiological Direction:
an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase] 1.14.14.1 -
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