Structure of PDB 2feu Chain A

Receptor sequence

>2feuA (length=404) Species: 303 (Pseudomonas putida)

LAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCNG
GHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQ
FRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPI
RIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIEQ
RRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFS
MEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHGV
QLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQ
HLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPAT
TKAV

3D structure

• PDB: 2feu The status of high-valent metal oxo complexes in the P450 cytochromes.
• Chain: A
• Resolution: 1.7 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): R176 G238 D241 T242 V243 C347 L348 G349 E356 V386
• 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	T101 R112 L244 G248 G249 T252 V295 D297 R299 Q322 T349 F350 G351 H355 C357 G359	T91 R102 L234 G238 G239 T242 V285 D287 R289 Q312 T339 F340 G341 H345 C347 G349
BS02	CAM	A	Y96 L244	Y86 L234

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