Structure of PDB 4a0m Chain A Binding Site BS01

Receptor Information
>4a0m Chain A (length=494) Species: 3562 (Spinacia oleracea) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FPIPARQLFIDGEWREPIKKNRIPVINPSTEEIIGDIPAATAEDVEVAVV
AARRAFRRNNWSATSGAHRATYLRAIAAKITEKKDHFVKLETIDSGKPFD
EAVLDIDDVASCFEYFAGQAEALDGKQKAPVTLPMERFKSHVLRQPLGVV
GLISPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLEFGEVCNEVG
LPPGVLNILTGLGPDAGAPLVSHPDVDKIAFTGSSATGSKVMASAAQLVK
PVTLELGGKSPIVVFEDVDIDKVVEWTIFGCFWTNGQICSATSRLLVHES
IAAEFVDKLVKWTKNIKISDPFEEGCRLGPVISKGQYDKIMKFISTAKSE
GATILYGGSRPEHLKKGYYIEPTIVTDISTSMQIWKEEVFGPVLCVKTFS
SEDEAIALANDTEYGLAAAVFSNDLERCERITKALEVGAVWVNCSQPCFV
QAPWGGIKRSGFGRELGEWGIQNYLNIKQVTQDISDEPWGWYKS
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain4a0m Chain A Residue 1498 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4a0m Amino Acid Residues Critical for the Specificity for Betaine Aldehyde of the Plant Aldh10 Isoenzyme Involved in the Synthesis of Glycine Betaine.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		I155 P157 W158 N159 M164 K182 E185 G215 A220 F233 T234 G235 S236 T239 E257 G259 C291 E390 F392 W456
Binding residue
(residue number reindexed from 1)		I153 P155 W156 N157 M162 K180 E183 G213 A218 F231 T232 G233 S234 T237 E255 G257 C289 E388 F390 W454
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N159 K182 E257 C291 E390 E467
Catalytic site (residue number reindexed from 1) N157 K180 E255 C289 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.
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:0006081 cellular aldehyde metabolic 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:4a0m, PDBe:4a0m, PDBj:4a0m
PDBsum4a0m
PubMed22345508
UniProtP17202|BADH_SPIOL Aminoaldehyde dehydrogenase BADH (Gene Name=BADH)

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