Structure of PDB 3iwj Chain A Binding Site BS02

Receptor Information
>3iwj Chain A (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 IDGOL
InChIInChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
InChIKeyPEDCQBHIVMGVHV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C(C(CO)O)O
ACDLabs 12.01
CACTVS 3.370		OCC(O)CO
FormulaC3 H8 O3
NameGLYCEROL;
GLYCERIN;
PROPANE-1,2,3-TRIOL
ChEMBLCHEMBL692
DrugBankDB09462
ZINCZINC000000895048
PDB chain3iwj Chain A Residue 506 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		D113 C453
Binding residue
(residue number reindexed from 1)		D110 C450
Annotation score1
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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