Structure of PDB 3up5 Chain B

Receptor sequence
>3up5B (length=532) Species: 303 (Pseudomonas putida) [Search protein sequence]
KSPALDAVVIGAGVTGIYQAFLINQAGMKVLGIEAGEDVGGTWYWNRYPG
CRLDTESYAYGYFALKGIIPEWEWSENFASQPEMLRYVNRAADAMDVRKH
YRFNTRVTAARYVENDRLWEVTLDNEEVVTCRFLISATGPLSASRMPDIK
GIDSFKGESFHSSRWPTDAEGAPKGVDFTGKRVGVIGTGATGVQIIPIAA
ETAKELYVFQRTPNWCTPLGNSPMSKEKMDSLRNRYPTILEYVKSTDTAF
PYHRDPRKGTDVSESERDAFFEELYRQPGYGIWLSGFRDLLLNKESNKFL
ADFVAKKIRQRVKDPVVAEKLIPKDHPFGAKRVPMETNYYETYNRDNVHL
VDIREAPIQEVTPEGIKTADAAYDLDVIIYATGFDAVTGSLDRIDIRGKD
NVRLIDAWAEGPSTYLGLQARGFPNFFTLVGPHNGSTFCNVGVCGGLQAE
WVLRMISYMKDNGFTYSEPTQAAENRWTEEVYADFSRTLLAEANAWWVKT
TRRTLVHVSGGPEYRKRCEQVAYNNYNGFELA
3D structure
PDB3up5 Cloning, Baeyer-Villiger biooxidations, and structures of the camphor pathway 2-oxo-{Delta}(3)-4,5,5-trimethylcyclopentenylacetyl-coenzyme A monooxygenase of Pseudomonas putida ATCC 17453.
ChainB
Resolution2.453 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.13.160: (2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA 1,5-monooxygenase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
GO:0050661 NADP binding
GO:0071949 FAD binding
Biological Process
GO:0019383 (+)-camphor catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3up5, PDBe:3up5, PDBj:3up5
PDBsum3up5
PubMed22267661
UniProtH3JQW0|OTEMO_PSEPU 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase (Gene Name=otemo)

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