Structure of PDB 3zqa Chain A

Receptor sequence
>3zqaA (length=489) Species: 287 (Pseudomonas aeruginosa) [Search protein sequence]
ARFEEQKLYIGGRYVEASSGATFETINPANGEVLAKVQRASREDVERAVQ
SAVEGQKVWAAMTAMQRSRILRRAVDILRERNDELAALETLDTGKPLAET
RSVDIVTGADVLEYYAGLVPAIEGEQIPLRETSFVYTRREPLGVVAGIGA
WNYPVQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYTEAGVPDGV
FNVLTGSGREVGQWLTEHPLIEKISFTGGTSTGKKVMASASSSSLKEVTM
ELGGKSPLIIFPDADLDRAADIAVMANFFSSGQVATNGTRVFIHRSQQAR
FEAKVLERVQRIRLGDPQDENTNFGPLVSFPHMESVLGYIESGKAQKARL
LCGGERVTDGAFGKGAYVAPTVFTDCRDDMTIVREEIFGPVMSILVYDDE
DEAIRRANDTEYGLAAGVVTQDLARAHRAIHRLEAGICWINTWGESPAEM
PVGGYKQSGVGRENGLTTLAHYTRIKSVQVELGDYASVF
3D structure
PDB3zqa Novel Nadph-Cysteine Covalent Adduct Found in the Active Site of an Aldehyde Dehydrogenase.
ChainA
Resolution2.45 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N153 K176 E252 A286 E387 E464
Catalytic site (residue number reindexed from 1) N152 K175 E251 A285 E386 E463
Enzyme Commision number 1.2.1.8: betaine-aldehyde dehydrogenase.
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 I149 G150 K176 S178 E179 S208 G209 F227 G229 G230 T233 V237 L253 G254 F389 I148 G149 K175 S177 E178 S207 G208 F226 G228 G229 T232 V236 L252 G253 F388
Gene Ontology
Molecular Function
GO:0008802 betaine-aldehyde dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0016620 oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
GO:0046872 metal ion binding
Biological Process
GO:0019285 glycine betaine biosynthetic process from choline

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3zqa, PDBe:3zqa, PDBj:3zqa
PDBsum3zqa
PubMed21732915
UniProtQ9HTJ1|BETB_PSEAE NAD/NADP-dependent betaine aldehyde dehydrogenase (Gene Name=betB)

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