Structure of PDB 2h7s Chain C

Receptor sequence
>2h7sC (length=405) Species: 303 (Pseudomonas putida) [Search protein sequence]
NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQR
QFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFP
IRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIE
QRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGALLVGGLDTVVNFLSF
SMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHG
VQLKKGDQILLPQMLSGLDERENAAPMHVDFSRQKVSHTTFGHGSHLCLG
QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPA
TTKAV
3D structure
PDB2h7s Cytochrome P450 active site plasticity: attenuation of imidazole binding in cytochrome P450cam by an L244A mutation.
ChainC
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G248 D251 C357 V396
Catalytic site (residue number reindexed from 1) G239 D242 C348 V387
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 HEC C Q108 R112 G248 T252 V253 D297 R299 T349 F350 H355 C357 G359 Q99 R103 G239 T243 V244 D288 R290 T340 F341 H346 C348 G350
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:2h7s, PDBe:2h7s, PDBj:2h7s
PDBsum2h7s
PubMed16943206
UniProtP00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)

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