Structure of PDB 6nbl Chain B

Receptor sequence

>6nblB (length=403) Species: 303 (Pseudomonas putida)

NLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRSN
GGHWIATRGQLIREAYEDYRHFSSESPFIPREAGEAYDFISMDPPEQRQF
RALANQVVGMPVVDKLENRIQELASSLIESLRPQGQCNFTEDYAEPFPIR
IFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIEQR
RQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFSM
EFLAKSPEHRQELIERPERIPAASEELLRRFSLVADGRILTSDYEFHGVQ
LKKGDQILLPQMLSGLDERENAAPMHVDFSRQCVSHTTFGHGSHLCLGQH
LARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATT
KAV

3D structure

• PDB: 6nbl Ligand and Redox Partner Binding Generates a New Conformational State in Cytochrome P450cam (CYP101A1).
• Chain: B
• Resolution: 2.15 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): R175 G237 D240 T241 V242 C346 L347 G348 E355 V385
• 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	R112 G249 T252 V253 V295 R299 T349 F350 H355 C357 L358 A363	R101 G238 T241 V242 V284 R288 T338 F339 H344 C346 L347 A352
BS02	CAM	B	E94 G248	E85 G237
BS03	CA	B	E198 D202	E187 D191

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:6nbl, PDBe:6nbl, PDBj:6nbl
• PDBsum: 6nbl
• PubMed: 30672701
• UniProt: P00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)