Structure of PDB 6we6 Chain B

Receptor sequence

>6we6B (length=405) Species: 303 (Pseudomonas putida)

NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCN
GGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQR
QFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFP
IRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIE
QRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLETVVNFLSF
SMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHG
VQLKKGDQILLPQMLSGLDERENAAPMHVDFSRQKVSHTTFGHGSHLCLG
QHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPA
TTKAV

3D structure

• PDB: 6we6 Proton Relay Network in the Bacterial P450s: CYP101A1 and CYP101D1.
• Chain: B
• Resolution: 2.16 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R186 E251 T252 C357 L358 G359
• Catalytic site (residue number reindexed from 1): R177 E242 T243 C348 L349 G350
• 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	B	T101 R112 G248 T252 D297 R299 Q322 F350 G351 H355 C357 G359	T92 R103 G239 T243 D288 R290 Q313 F341 G342 H346 C348 G350
BS02	CAM	B	Y96 L244	Y87 L235

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:6we6, PDBe:6we6, PDBj:6we6
• PDBsum: 6we6
• PubMed: 32574066
• UniProt: P00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)