Structure of PDB 2jbs Chain D

Receptor sequence
>2jbsD (length=400) Species: 470 (Acinetobacter baumannii) [Search protein sequence]
IRLVYTHAQTPDVSGVSMLEKIQQILPQIAKNAESAEQLRRVPDENIKLL
KEIGLHRAFQPKVYGGLEMSLPDFANCIVTLAGACAGTAWAFSLLCTHSH
QIAMFSKQLQDEIWLKDPDATASSSIAPFGKVEEVEGGIILNGDYGWSSG
CDHAEYAIVGFNRFDADGNKIYSFGVIPRSDYEIVDNWYAQAIKSSGSKM
LKLVNVFIPEYRISKAKDMMEGKSAGFGLYPDSKIFYTPYRPYFASGFSA
VSLGIAERMIEAFKEKQRNRVRAYTGANVGLATPALMRIAESTHQVAAAR
ALLEKTWEDHRIHGLNHQYPNKETLAFWRTNQAYAVKMCIEAVDRLMAAA
GATSFMDNSELQRLFRDAHMTGAHAYTDYDVCAQILGRELMGMEPDPTMV
3D structure
PDB2jbs Structure of the Monooxygenase Component of a Two-Component Flavoprotein Monooxygenase.
ChainD
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 D G373 A374 T375 G351 A352 T353
BS02 FMN D W112 L116 S146 I148 W169 S170 S171 M392 H396 A397 W90 L94 S124 I126 W147 S148 S149 M370 H374 A375
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:2jbs, PDBe:2jbs, PDBj:2jbs
PDBsum2jbs
PubMed17227849
UniProtQ6Q272|HPAH_ACIBA p-hydroxyphenylacetate 3-hydroxylase, oxygenase component (Gene Name=C2-hpah)

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