Structure of PDB 2m56 Chain A

Receptor sequence
>2m56A (length=404) Species: 303 (Pseudomonas putida) [Search protein sequence]
LAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCNG
GHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQ
FRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPI
RIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIEQ
RRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFS
MEFLAKSPEHRQELIQRPERIPAACEELLRRFSLVADGRILTSDYEFHGV
QLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQ
HLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPAT
TKAV
3D structure
PDB2m56 The structure of the cytochrome p450cam-putidaredoxin complex determined by paramagnetic NMR spectroscopy and crystallography.
ChainA
ResolutionN/A
3D
structure
Catalytic site residues are labeled in the structure
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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
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 P100 T101 R112 L245 G248 T252 V295 D297 R299 Q322 T349 F350 G351 H355 C357 P90 T91 R102 L235 G238 T242 V285 D287 R289 Q312 T339 F340 G341 H345 C347
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

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Cellular Component
External links
PDB RCSB:2m56, PDBe:2m56, PDBj:2m56
PDBsum2m56
PubMed23856620
UniProtP00183|CPXA_PSEPU Camphor 5-monooxygenase (Gene Name=camC)

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