Structure of PDB 1re9 Chain A

Receptor sequence

>1re9A (length=404) Species: 303 (Pseudomonas putida)

LAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCNG
GHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQ
FRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPI
RIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIEQ
RRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFS
MEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHGV
QLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQ
HLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPAT
TKAV

3D structure

• PDB: 1re9 Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires.
• Chain: A
• Resolution: 1.45 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R176 G238 D241 T242 V243 C347 L348 G349 E356 V386
• 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	HEM	A	P90 T91 R102 L234 G238 G239 T242 D287 R289 Q312 F340 G341 H345 C347 G349	P90 T91 R102 L234 G238 G239 T242 D287 R289 Q312 F340 G341 H345 C347 G349
BS02	DSO	A	Y19 F77 P79 Y86 P177 F183 I385	Y19 F77 P79 Y86 P177 F183 I385	MOAD: Kd~0.02uM

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:1re9, PDBe:1re9, PDBj:1re9
• PDBsum: 1re9
• PubMed: 15522298
• UniProt: P00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)