Structure of PDB 4v37 Chain A

Receptor sequence
>4v37A (length=495) Species: 3562 (Spinacia oleracea) [Search protein sequence]
FPIPARQLFIDGEWREPIKKNRIPVINPSTEEIIGDIPAATAEDVEVAVV
AARRAFRRNNWSATSGAHRATYLRAIAAKITEKKDHFVKLETIDSGKPFD
EAVLDIDDVASCFEYFAGQAEALDGKQKAPVTLPMERFKSHVLRQPLGVV
GLISPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLEFGEVCNEVG
LPPGVLNILTGLGPDAGAPLVSHPDVDKIAFTGSSATGSKVMASAAQLVK
PVTLELGGKSPIVVFEDVDIDKVVEWTIFGCFWTNGQIASATSRLLVHES
IAAEFVDKLVKWTKNIKISDPFEEGCRLGPVISKGQYDKIMKFISTAKSE
GATILYGGSRPEHLKKGYYIEPTIVTDISTSMQIWKEEVFGPVLCVKTFS
SEDEAIALANDTEYGLAAAVFSNDLERCERITKALEVGAVWVNCSQPCFV
QAPWGGIKRSGFGRELGEWGIQNYLNIKQVTQDISDEPWGWYKSP
3D structure
PDB4v37 Identification of a Stable Thiohemiacetal Involving a Conserved Cysteine in the Substrate Inactivation of S. Oleracea Betaine Aldehyde Dehydrogenase
ChainA
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) N157 K180 E255 A289 E388 E465
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 A I155 S156 P157 W158 N159 M164 K182 S184 E185 G215 G219 A220 T234 G235 S236 T239 E257 L258 A291 E390 F392 I153 S154 P155 W156 N157 M162 K180 S182 E183 G213 G217 A218 T232 G233 S234 T237 E255 L256 A289 E388 F390
BS02 0D8 A C450 W456 C448 W454
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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