Structure of PDB 3up4 Chain A

Receptor sequence
>3up4A (length=528) Species: 303 (Pseudomonas putida) [Search protein sequence]
KSPALDAVVIGAGVTGIYQAFLINQAGMKVLGIEAGEDVGGTWYWNRYPG
CRLDTESYAYGYFALKGIIPEWEWSENFASQPEMLRYVNRAADAMDVRKH
YRFNTRVTAARYVENDRLWEVTLDNEEVVTCRFLISATGPLSASRMPDIK
GIDSFKGESFHSSRWPTGAPKGVDFTGKRVGVIGTGATGVQIIPIAAETA
KELYVFQRTPNWCTPLGNSPMSKEKMDSLRNRYPTILEYVKSTDTAFPYH
RDPRKGTDVSESERDAFFEELYRQPGYGIWLSGFRDLLLNKESNKFLADF
VAKKIRQRVKDPVVAEKLIPKDHPFGAKRVPMETNYYETYNRDNVHLVDI
REAPIQEVTPEGIKTADAAYDLDVIIYATGFDAVTGSLDRIDIRGKDNVR
LIDAWAEGPSTYLGLQARGFPNFFTLVGPHNGSTFCNVGVCGGLQAEWVL
RMISYMKDNGFTYSEPTQAAENRWTEEVYADFSRTLLAEANAWWVKTRRT
LVHVSGGPEYRKRCEQVAYNNYNGFELA
3D structure
PDB3up4 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.
ChainA
Resolution2.804 Å
3D
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
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3up4, PDBe:3up4, PDBj:3up4
PDBsum3up4
PubMed22267661
UniProtH3JQW0|OTEMO_PSEPU 2-oxo-Delta(3)-4,5,5-trimethylcyclopentenylacetyl-CoA monooxygenase (Gene Name=otemo)

[Back to BioLiP]