Structure of PDB 1phd Chain A Binding Site BS02

Receptor Information
>1phd Chain A (length=405) Species: 303 (Pseudomonas putida) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQR
QFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFP
IRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIE
QRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSF
SMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHG
VQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLG
QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPA
TTKAV
Ligand information
Ligand IDPIW
InChIInChI=1S/C9H8N2/c1-2-4-9(5-3-1)11-7-6-10-8-11/h1-8H
InChIKeySEULWJSKCVACTH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370
OpenEye OEToolkits 1.7.0		c1ccc(cc1)n2ccnc2
ACDLabs 12.01n2ccn(c1ccccc1)c2
FormulaC9 H8 N2
Name1-phenyl-1H-imidazole
ChEMBLCHEMBL275066
DrugBank
ZINCZINC000000160340
PDB chain1phd Chain A Residue 422 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1phd Crystal structures of metyrapone- and phenylimidazole-inhibited complexes of cytochrome P-450cam.
Resolution1.6 Å
Binding residue
(original residue number in PDB)		F87 G248 T252
Binding residue
(residue number reindexed from 1)		F78 G239 T243
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R186 G248 D251 T252 V253 C357 L358 G359 E366 V396
Catalytic site (residue number reindexed from 1) R177 G239 D242 T243 V244 C348 L349 G350 E357 V387
Enzyme Commision number 1.14.15.1: camphor 5-monooxygenase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0005515 protein binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0018683 camphor 5-monooxygenase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0019383 (+)-camphor catabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1phd, PDBe:1phd, PDBj:1phd
PDBsum1phd
PubMed3442650
UniProtP00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)

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