Structure of PDB 1gek Chain A

Receptor sequence
>1gekA (length=406) Species: 303 (Pseudomonas putida) [Search protein sequence]
ANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRC
NGGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQ
RQFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPF
PIRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPII
EQRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLS
FSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFH
GVQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCL
GQHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDP
ATTKAV
3D structure
PDB1gek Structural characterization of n-butyl-isocyanide complexes of cytochromes P450nor and P450cam.
ChainA
Resolution1.7 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
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A T101 R112 L245 G248 T252 D297 R299 Q322 T349 F350 G351 H355 C357 L358 G359 T93 R104 L237 G240 T244 D289 R291 Q314 T341 F342 G343 H347 C349 L350 G351
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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Cellular Component
External links
PDB RCSB:1gek, PDBe:1gek, PDBj:1gek
PDBsum1gek
PubMed11258878
UniProtP00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)

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