Structure of PDB 3fwf Chain A

Receptor sequence

>3fwfA (length=404) Species: 303 (Pseudomonas putida)

LAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCNG
GHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQ
FRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPI
RIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIEQ
RRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFS
MEFLAKSPEHRQELIQRPERIPAACEELLRRFSLVADGRILTSDYEFHGV
QLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQ
HLARLQIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPAT
TKAV

3D structure

• PDB: 3fwf Probing the role of the proximal heme ligand in cytochrome P450cam by recombinant incorporation of selenocysteine.
• Chain: A
• Resolution: 1.83 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R186 G248 D251 T252 V253 C357 L358 G359 Q366 V396
• Catalytic site (residue number reindexed from 1): R176 G238 D241 T242 V243 C347 L348 G349 Q356 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	HEM	A	T101 R112 L245 G248 T252 D297 R299 Q322 T349 F350 G351 H355 U357	T91 R102 L235 G238 T242 D287 R289 Q312 T339 F340 G341 H345 U347
BS02	CAM	A	F87 Y96 L244	F77 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:3fwf, PDBe:3fwf, PDBj:3fwf
• PDBsum: 3fwf
• PubMed: 19293375
• UniProt: P00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)