Structure of PDB 2jbt Chain C

Receptor sequence
>2jbtC (length=399) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
RLVYTHAQTPDVSGVSMLEKIQQILPQIAKNAESAEQLRRVPDENIKLLK
EIGLHRAFQPKVYGGLEMSLPDFANCIVTLAGACAGTAWAFSLLCTHSHQ
IAMFSKQLQDEIWLKDPDATASSSIAPFGKVEEVEGGIILNGDYGWSSGC
DHAEYAIVGFNRFDADGNKIYSFGVIPRSDYEIVDNWYAQAIKSSGSKML
KLVNVFIPEYRISKAKDMMEGKSAGFGLYPDSKIFYTPYRPYFASGFSAV
SLGIAERMIEAFKEKQRNRVRAYTGANVGLATPALMRIAESTHQVAAARA
LLEKTWEDHRIHGLNHQYPNKETLAFWRTNQAYAVKMCIEAVDRLMAAAG
ATSFMDNSELQRLFRDAHMTGAHAYTDYDVCAQILGRELMGMEPDPTMV
3D structure
PDB2jbt Structure of the Monooxygenase Component of a Two-Component Flavoprotein Monooxygenase.
ChainC
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.14.14.9: 4-hydroxyphenylacetate 3-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 FMN C Y296 G373 A374 T375 Y273 G350 A351 T352
BS02 FMN C W112 S146 S147 I148 W169 S170 S171 M392 H396 A397 W89 S123 S124 I125 W146 S147 S148 M369 H373 A374
BS03 4HP C L116 I148 R263 F266 A267 Y398 L93 I125 R240 F243 A244 Y375
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003995 acyl-CoA dehydrogenase activity
GO:0004497 monooxygenase activity
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors
GO:0050660 flavin adenine dinucleotide binding
GO:0052881 4-hydroxyphenylacetate 3-monooxygenase activity
Biological Process
GO:0009056 catabolic process
GO:0033539 fatty acid beta-oxidation using acyl-CoA dehydrogenase
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2jbt, PDBe:2jbt, PDBj:2jbt
PDBsum2jbt
PubMed17227849
UniProtQ6Q272|HPAH_ACIBA p-hydroxyphenylacetate 3-hydroxylase, oxygenase component (Gene Name=C2-hpah)

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