Structure of PDB 3wrh Chain E

Receptor sequence
>3wrhE (length=405) Species: 303 (Pseudomonas putida) [Search protein sequence]
NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQR
QFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFP
IRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIE
QRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSF
SMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHG
VQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLG
QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPA
TTKAV
3D structure
PDB3wrh Structure of P450cam intermedite
ChainE
Resolution1.62 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 HEM E P100 T101 R112 G248 T252 V295 D297 R299 Q322 T349 F350 G351 H355 C357 G359 P91 T92 R103 G239 T243 V286 D288 R290 Q313 T340 F341 G342 H346 C348 G350
BS02 CAM E Y96 L244 Y87 L235
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:3wrh, PDBe:3wrh, PDBj:3wrh
PDBsum3wrh
PubMed
UniProtP00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)

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