Structure of PDB 8uzo Chain D

Receptor sequence
>8uzoD (length=486) Species: 1028307 (Klebsiella aerogenes KCTC 2190) [Search protein sequence]
AEQQLYIHGKFVAATSGKTFETINPATGEVLATVQAAGREDVDRAVKSAQ
QGQKVWAAMSAMARSRILRKAVDILRERNDELARLETLDTGKPLSETAAV
DIVTGADVLEYYAGLIPALEGSQIPLRDSSFVYTRREPLGVVAGIGAWNY
PIQIALWKSAPALAAGNAMIFKPSEVTPLTALKLAEIYREAGLPDGVFNV
LPGIGAETGQYLTEHPDIAKISFTGGVASGKKVMANSAASSLKEVTMELG
GKSPLIIAEDANLDLAADIAMMANFYSSGQVCTNGTRVFVPAKFKAEFEH
KILERVGRIRAGDLFADDTNFGPLVSFPHRQNVLRYIESGKSEGARLLCG
GDVLKGEGFDNGAWVAPTVFTDCTDDMTIVREEIFGPVMSILSYDDEAEV
IRRANATEYGLAAGVVTPDLNRAHRIIHQLEAGICWINSWGESPAEMPVG
GYKHSGIGRENGVMTLQSYTQVKSIQVEMGPFQSIF
3D structure
PDB8uzo Crystal Structure of Betaine aldehyde dehydrogenase (BetB) from Klebsiella aerogenes (ADP bound)
ChainD
Resolution2.1 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 ADP D I149 G150 W152 K176 E179 G209 G213 F227 G229 G230 S233 K236 V237 I145 G146 W148 K172 E175 G205 G209 F223 G225 G226 S229 K232 V233
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

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Molecular Function
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Biological Process
External links
PDB RCSB:8uzo, PDBe:8uzo, PDBj:8uzo
PDBsum8uzo
PubMed
UniProtA0A0H3FPU4

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