Structure of PDB 2vro Chain A

Receptor sequence
>2vroA (length=521) Species: 266265 (Paraburkholderia xenovorans LB400) [Search protein sequence]
HMTELLKNHVAGQWIAGTGAGITLTDPVTGVALVRVSSEGLDLARAFSFA
REDGGAALRALTYAQRAARLADIVKLLQAKRGDYYAIATANSGTTRNDSA
VDIDGGIFTLSYYAKLGASLGEVHALRDGSAESLSKDRSFSAQHVLSPTR
GVALFINAFNFPSWGLWEKAAPALLSGVPVIVKPATATAWLTQRMVADVV
DAGILPPGALSIICGSSAGLLDQIRSFDVVSFTGSADTAATLRAHPAFVQ
RGARLNVEADSLNSAILCADATPDTPAFDLFIKEVVREMTVKSGQKCTAI
RRAFVPEAALEPVLEALKAKLAKITVGNPRNDAVRMGSLVSREQYENVLA
GIAALREEAVLAYDSSAVPLIDADANIAACVAPHLFVVNDPDNATLLHDV
EVFGPVASVAPYRVTTDTLPEAHAVALARRGQGSLVASIYSNDDAHLGRL
ALELADSHGRVHAISPSVQHSQTGHGNVMPMSLHGGPGRAGGGEELGGLR
ALAFYHRRSAIQAASAAIGTL
3D structure
PDB2vro Structural and Biochemical Characterization of a Novel Aldehyde Dehydrogenase Encoded by the Benzoate Oxidation (Box) Pathway in Burkholderia Xenovorans Lb400
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N159 K182 E257 C296 E400 L497
Catalytic site (residue number reindexed from 1) N160 K183 E258 C297 E401 L496
Enzyme Commision number 1.2.1.-
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 NDP A I155 K182 S216 S234 T237 L241 F402 I156 K183 S217 S235 T238 L242 F403
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

View graph for
Molecular Function
External links
PDB RCSB:2vro, PDBe:2vro, PDBj:2vro
PDBsum2vro
PubMed18462753
UniProtQ13WK4

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