Structure of PDB 4ek1 Chain A

Receptor sequence
>4ek1A (length=403) Species: 303 (Pseudomonas putida) [Search protein sequence]
LAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQECNVPDLVWTRSNG
GHWIATRGQLIREAYEDYRHFSSESPFIPREAGEAYDFIPTSMDPPEQRQ
FRALANQVVGMPVVDKLENRIQELASSLIESLRPQGQCNFTEDYAEPFPI
RIFMLLAGLPEEDIPHLKYLTDQMTRPDGCMTFAEAKEALYDYLIPIIEQ
RRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFS
MEFLAKSPEHRQELIERPERIPAASEELLRRFSLVADGRILTSDYEFHGV
QLKKGDQILLPQMLSGLDERENAAPMHVDFSRQKVSHTTFGHGSHLCLGQ
HLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPAT
TKA
3D structure
PDB4ek1 Double electron-electron resonance shows cytochrome P450cam undergoes a conformational change in solution upon binding substrate.
ChainA
Resolution1.97 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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) R176 G238 D241 T242 V243 C347 L348 G349 E356 V386
Enzyme Commision number 1.14.15.1: camphor 5-monooxygenase.
Interaction with ligand
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:4ek1, PDBe:4ek1, PDBj:4ek1
PDBsum4ek1
PubMed22826259
UniProtP00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)

[Back to BioLiP]