Structure of PDB 4v37 Chain D

Receptor sequence
>4v37D (length=493) Species: 3562 (Spinacia oleracea) [Search protein sequence]
PIPARQLFIDGEWREPIKKNRIPVINPSTEEIIGDIPAATAEDVEVAVVA
ARRAFRRNNWSATSGAHRATYLRAIAAKITEKKDHFVKLETIDSGKPFDE
AVLDIDDVASCFEYFAGQAEALDGKQKAPVTLPMERFKSHVLRQPLGVVG
LISPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLEFGEVCNEVGL
PPGVLNILTGLGPDAGAPLVSHPDVDKIAFTGSSATGSKVMASAAQLVKP
VTLELGGKSPIVVFEDVDIDKVVEWTIFGCFWTNGQIASATSRLLVHESI
AAEFVDKLVKWTKNIKISDPFEEGCRLGPVISKGQYDKIMKFISTAKSEG
ATILYGGSRPEHLKKGYYIEPTIVTDISTSMQIWKEEVFGPVLCVKTFSS
EDEAIALANDTEYGLAAAVFSNDLERCERITKALEVGAVWVNCSQPCFVQ
APWGGIKRSGFGRELGEWGIQNYLNIKQVTQDISDEPWGWYKS
3D structure
PDB4v37 Identification of a Stable Thiohemiacetal Involving a Conserved Cysteine in the Substrate Inactivation of S. Oleracea Betaine Aldehyde Dehydrogenase
ChainD
Resolution2.1 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 A291 E390 E467
Catalytic site (residue number reindexed from 1) N156 K179 E254 A288 E387 E464
Enzyme Commision number 1.2.1.-
1.2.1.19: aminobutyraldehyde dehydrogenase.
1.2.1.47: 4-trimethylammoniobutyraldehyde dehydrogenase.
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 NAD D I155 S156 P157 W158 N159 M164 K182 E185 G215 G219 A220 T234 G235 S236 T239 E257 L258 A291 E390 F392 I152 S153 P154 W155 N156 M161 K179 E182 G212 G216 A217 T231 G232 S233 T236 E254 L255 A288 E387 F389
BS02 0D8 D W167 S292 C450 W456 W164 S289 C447 W453
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:0019145 aminobutyraldehyde dehydrogenase (NAD+) activity
GO:0030955 potassium ion binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0047105 4-trimethylammoniobutyraldehyde dehydrogenase activity
Biological Process
GO:0019285 glycine betaine biosynthetic process from choline
GO:0110095 cellular detoxification of aldehyde

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4v37, PDBe:4v37, PDBj:4v37
PDBsum4v37
PubMed
UniProtP17202|BADH_SPIOL Aminoaldehyde dehydrogenase BADH (Gene Name=BADH)

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