Structure of PDB 3iwj Chain B Binding Site BS01

Receptor Information
>3iwj Chain B (length=500) Species: 3888 (Pisum sativum) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PIPTRQLFINGDWKAPVLNKRIPVINPATQNIIGDIPAATKEDVDVAVAA
AKTALTRNKGADWATASGAVRARYLRAIAAKVTEKKPELAKLESIDCGKP
LDEAAWDIDDVAGCFEYYADLAEKLDARQKAPVSLPMDTFKSHVLREPIG
VVGLITPWNYPMLMATWKVAPALAAGCAAILKPSELASLTCLELGEICKE
VGLPPGVLNILTGLGPEAGAPLATHPDVDKVAFTGSSATGSKIMTAAAQL
VKPVSLELGGKSPLVVFEDVDLDKAAEWAIFGCFWTNGQICSATSRLILH
ESIATEFLNRIVKWIKNIKISDPLEEGCRLGPVVSEGQYEKILKFVSNAK
SEGATILTGGSRPEHLKKGFFIEPTIITDVTTNMQIWREEVFGPVLCVKT
FSTEEEAIDLANDTVYGLGAAVISNDLERCERVTKAFKAGIVWVNCSQPC
FTQAPWGGVKRSGFGRELGEWGLDNYLSVKQVTQYISEEPWGWYQPPAKL
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 chain3iwj Chain B Residue 504 [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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PDB3iwj Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes.
Resolution2.15 Å
Binding residue
(original residue number in PDB)		I158 T159 W161 K185 S187 E188 G218 G222 A223 F236 S239 T242 I246
Binding residue
(residue number reindexed from 1)		I155 T156 W158 K182 S184 E185 G215 G219 A220 F233 S236 T239 I243
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N162 K185 E260 C294 E393 E470
Catalytic site (residue number reindexed from 1) N159 K182 E257 C291 E390 E467
Enzyme Commision number 1.2.1.-
1.2.1.19: aminobutyraldehyde dehydrogenase.
1.2.1.54: gamma-guanidinobutyraldehyde dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0031402 sodium ion binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0047107 gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity
Biological Process
GO:0019285 glycine betaine biosynthetic process from choline
GO:0110095 cellular detoxification of aldehyde
Cellular Component
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3iwj, PDBe:3iwj, PDBj:3iwj
PDBsum3iwj
PubMed20026072
UniProtQ93YB2|AADH2_PEA Aminoaldehyde dehydrogenase 2, peroxisomal (Gene Name=AMADH2)

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