Structure of PDB 8vqw Chain D

Receptor sequence
>8vqwD (length=487) Species: 1028307 (Klebsiella aerogenes KCTC 2190) [Search protein sequence]
MAEQQLYIHGKFVAATSGKTFETINPATGEVLATVQAAGREDVDRAVKSA
QQGQKVWAAMSAMARSRILRKAVDILRERNDELARLETLDTGKPLSETAA
VDIVTGADVLEYYAGLIPALEGSQIPLRDSSFVYTRREPLGVVAGIGAWN
YPIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYREAGLPDGVFN
VLPGIGAETGQYLTEHPDIAKISFTGGVASGKKVMANSAASSLKEVTMEL
GGKSPLIIAEDANLDLAADIAMMANFYSSGQVCTNGTRVFVPAKFKAEFE
HKILERVGRIRAGDLFADDTNFGPLVSFPHRQNVLRYIESGKSEGARLLC
GGDVLKGEGFDNGAWVAPTVFTDCTDDMTIVREEIFGPVMSILSYDDEAE
VIRRANATEYGLAAGVVTPDLNRAHRIIHQLEAGICWINSWGESPAEMPV
GGYKHSGIGRENGVMTLQSYTQVKSIQVEMGPFQSIF
3D structure
PDB8vqw Crystal Structure of Betaine aldehyde dehydrogenase (BetB) from Klebsiella aerogenes (CoA bound)
ChainD
Resolution2.2 Å
3D
structure
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Enzymatic activity
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 COA D S178 E179 G209 A232 S233 K236 S175 E176 G206 A229 S230 K233
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:8vqw, PDBe:8vqw, PDBj:8vqw
PDBsum8vqw
PubMed
UniProtA0A0H3FPU4

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