Structure of PDB 1k2o Chain B

Receptor sequence
>1k2oB (length=406) Species: 303 (Pseudomonas putida) [Search protein sequence]
ANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRC
NGGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQ
RQFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPF
PIRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPII
EQRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLS
FSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFH
GVQLKKGDQILLPQMLSGLDERENAAPMHVDFSRQKVSHTTFGHGSHLCL
GQHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDP
ATTKAV
3D structure
PDB1k2o Probing the open state of cytochrome P450cam with ruthenium-linker substrates.
ChainB
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
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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) R178 G240 D243 T244 V245 C349 L350 G351 E358 V388
Enzyme Commision number 1.14.15.1: camphor 5-monooxygenase.
Interaction with ligand
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:1k2o, PDBe:1k2o, PDBj:1k2o
PDBsum1k2o
PubMed11606730
UniProtP00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)

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