Structure of PDB 7cpp Chain A

Receptor sequence

>7cppA (length=405) Species: 303 (Pseudomonas putida)

NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQR
QFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFP
IRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIE
QRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSF
SMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHG
VQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLG
QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPA
TTKAV

3D structure

• PDB: 7cpp The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM.
• Chain: A
• Resolution: 2.0 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	HEM	A	T101 R112 T252 D297 R299 Q322 T349 F350 H355 C357 G359	T92 R103 T243 D288 R290 Q313 T340 F341 H346 C348 G350
BS02	NCM	A	F87 Y96	F78 Y87

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:7cpp, PDBe:7cpp, PDBj:7cpp
• PDBsum: 7cpp
• PubMed: 2713354
• UniProt: P00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)