Structure of PDB 3iwk Chain E

Receptor sequence
>3iwkE (length=496) Species: 3888 (Pisum sativum) [Search protein sequence]
SRQLFIDGEWRVPILNKRIPNINPSTENIIGDIPAATKEDVDLAVDAAKR
AISRKNGRDWSAASGSLRARYLRAIAAKIKEKKDELGKLESIDCGKPLEE
ALADLDDVVACFEYYAGLAEELDSKQKAPISLPMDTFKSYILKEPIGVVA
LITPWNYPFLMATWKIAPALAAGCAAILKPSELASVTCLELGEICKEVGL
PRGVLNIVTGLGHEAGASLASHPDVDKISFTGSSATGSKIMTTAAQLVKP
VSLELGGKSPIVVFEDVDLDKVAEWTVFGCFFTNGQICSATSRLIVHESI
AVEFVDKLVKWAENIKISDPLEEGCRLGPIVSEAQYKKVLNCISSAKSEG
ATILTGGRRPEHLKKGYFVEPTIITDVTTSMQIWREEVFGPVLAVKTFST
EEEAINLANDTHYGLGSAVMSNDLERCERLSKALQAGIVWINCAQPSFIQ
APWGGIKRSGFGRELGEWGLENYLSVKQVTRYTSDEPWGWYQPPSK
3D structure
PDB3iwk Structural and functional characterization of plant aminoaldehyde dehydrogenase from Pisum sativum with a broad specificity for natural and synthetic aminoaldehydes.
ChainE
Resolution2.4 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) N156 K179 E254 C288 E387 E464
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 E P160 W161 G218 G222 A223 G238 S239 T242 K245 I246 C294 Q341 E393 F395 P154 W155 G212 G216 A217 G232 S233 T236 K239 I240 C288 Q335 E387 F389
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:3iwk, PDBe:3iwk, PDBj:3iwk
PDBsum3iwk
PubMed20026072
UniProtQ8VWZ1|AADH1_PEA Aminoaldehyde dehydrogenase 1, peroxisomal (Gene Name=AMADH1)

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