Structure of PDB 5cpp Chain A Binding Site BS02

Receptor Information
>5cpp 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 IDADO
InChIInChI=1S/C10H14O/c11-10-8-2-6-1-7(4-8)5-9(10)3-6/h6-9H,1-5H2/t6-,7+,8-,9+
InChIKeyIYKFYARMMIESOX-SPJNRGJMSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1C2CC3CC1CC(C2)C3=O
CACTVS 3.341O=C1C2CC3CC(C2)CC1C3
ACDLabs 10.04O=C1C2CC3CC1CC(C2)C3
FormulaC10 H14 O
NameADAMANTANONE
ChEMBL
DrugBankDB02125
ZINC
PDB chain5cpp Chain A Residue 422 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5cpp The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM.
Resolution2.08 Å
Binding residue
(original residue number in PDB)		Y96 L244 V247
Binding residue
(residue number reindexed from 1)		Y87 L235 V238
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5cpp, PDBe:5cpp, PDBj:5cpp
PDBsum5cpp
PubMed2713354
UniProtP00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)

[Back to BioLiP]