Structure of PDB 3wrk Chain D

Receptor sequence
>3wrkD (length=392) Species: 303 (Pseudomonas putida) [Search protein sequence]
NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPRPEQRQFRALANQVVGMPVV
DKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDI
PHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVA
NGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFSMEFLAKSPEHRQEL
IERPERIPAACEELLRRFSLVADGRILTSDYEFHGVQLKKGDQILLPQML
SGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQHLARREIIVTLKEW
LTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAVHH
3D structure
PDB3wrk Structure of P450cam intermedite
ChainD
Resolution2.609 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) G224 D227 C333 V372
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 D R112 L245 G248 G249 T252 V295 D297 R299 Q322 T349 F350 G351 H355 C357 G359 R88 L221 G224 G225 T228 V271 D273 R275 Q298 T325 F326 G327 H331 C333 G335
BS02 CAM D F87 G248 F78 G224
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:3wrk, PDBe:3wrk, PDBj:3wrk
PDBsum3wrk
PubMed
UniProtP00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)

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