Structure of PDB 2qbn Chain A

Receptor sequence

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

NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQR
QFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFP
IRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIE
QRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVVGLDTVVNFLSF
SMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHG
VQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLG
QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPA
TTKAV

3D structure

• PDB: 2qbn Alteration of P450 Distal Pocket Solvent Leads to Impaired Proton Delivery and Changes in Heme Geometry.
• Chain: A
• Resolution: 1.75 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R186 V248 D251 T252 V253 C357 L358 G359 E366 V396
• Catalytic site (residue number reindexed from 1): R177 V239 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 L244 V248 T252 D297 R299 Q322 F350 G351 H355 C357 G359	T92 R103 L235 V239 T243 D288 R290 Q313 F341 G342 H346 C348 G350
BS02	CAM	A	Y96 V248 V295	Y87 V239 V286

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:2qbn, PDBe:2qbn, PDBj:2qbn
• PDBsum: 2qbn
• PubMed: 18001135
• UniProt: P00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)