Structure of PDB 2fe6 Chain A

Receptor sequence

>2fe6A (length=405) Species: 303 (Pseudomonas putida)

NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQR
QFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFP
IRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIE
QRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSF
SMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHG
VQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLG
QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPA
TTKAV

3D structure

• PDB: 2fe6 The status of high-valent metal oxo complexes in the P450 cytochromes.
• Chain: A
• Resolution: 1.5 Å

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): R177 G239 D242 T243 V244 C348 L349 G350 E357 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	MNR	A	P100 T101 R112 G248 T252 D297 R299 Q322 T349 F350 G351 H355 C357 G359	P91 T92 R103 G239 T243 D288 R290 Q313 T340 F341 G342 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

External links

• PDB: RCSB:2fe6, PDBe:2fe6, PDBj:2fe6
• PDBsum: 2fe6
• PubMed: 16510191
• UniProt: P00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)