Structure of PDB 3iwj Chain A

Receptor sequence
>3iwjA (length=500) Species: 3888 (Pisum sativum) [Search protein sequence]
PIPTRQLFINGDWKAPVLNKRIPVINPATQNIIGDIPAATKEDVDVAVAA
AKTALTRNKGADWATASGAVRARYLRAIAAKVTEKKPELAKLESIDCGKP
LDEAAWDIDDVAGCFEYYADLAEKLDARQKAPVSLPMDTFKSHVLREPIG
VVGLITPWNYPMLMATWKVAPALAAGCAAILKPSELASLTCLELGEICKE
VGLPPGVLNILTGLGPEAGAPLATHPDVDKVAFTGSSATGSKIMTAAAQL
VKPVSLELGGKSPLVVFEDVDLDKAAEWAIFGCFWTNGQICSATSRLILH
ESIATEFLNRIVKWIKNIKISDPLEEGCRLGPVVSEGQYEKILKFVSNAK
SEGATILTGGSRPEHLKKGFFIEPTIITDVTTNMQIWREEVFGPVLCVKT
FSTEEEAIDLANDTVYGLGAAVISNDLERCERVTKAFKAGIVWVNCSQPC
FTQAPWGGVKRSGFGRELGEWGLDNYLSVKQVTQYISEEPWGWYQPPAKL
3D structure
PDB3iwj Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes.
ChainA
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 I158 T159 W161 K185 S187 E188 G218 A223 F236 G238 S239 T242 I246 I155 T156 W158 K182 S184 E185 G215 A220 F233 G235 S236 T239 I243
BS02 GOL A D113 C453 D110 C450
BS03 GOL A Y163 W170 I293 C294 W459 Y160 W167 I290 C291 W456
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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