Structure of PDB 4i8p Chain A

Receptor sequence
>4i8pA (length=500) Species: 4577 (Zea mays) [Search protein sequence]
MVPLRQLFVDGEWRPPAQGRRLPVVNPTTEAHIGEIPAGTAEDVDAAVAA
ARAALKRNRGRDWARAPGAVRAKYLRAIAAKVIERKPELAKLEALDCGKP
YDEAAWDMDDVAGCFEYFADQAEALDKRQNSPVSLPMETFKCHLRREPIG
VVGLITPWNYPLLMATWKIAPALAAGCTAVLKPSELASVTCLELADICKE
VGLPSGVLNIVTGLGPDAGAPLSAHPDVDKVAFTGSFETGKKIMASAAPM
VKPVTLELGGKSPIVVFDDVDIDKAVEWTLFGCFWTNGQICSATSRLLIH
TKIAKKFNERMVAWAKNIKVSDPLEEGCRLGPVVSEGQYEKIKKFISNAK
SQGATILTGGVRPAHLEKGFFIEPTIITDITTSMEIWREEVFGPVLCVKE
FSTEDEAIELANDTQYGLAGAVISGDRERCQRLSEEIDAGCIWVNCSQPC
FCQAPWGGNKRSGFGRELGEGGIDNYLSVKQVTEYISDEPWGWYQSPSKL
3D structure
PDB4i8p Plant ALDH10 family: identifying critical residues for substrate specificity and trapping a thiohemiacetal intermediate.
ChainA
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N164 K187 E262 C296 E395 E472
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.
1.2.1.47: 4-trimethylammoniobutyraldehyde dehydrogenase.
1.2.1.54: gamma-guanidinobutyraldehyde dehydrogenase.
1.2.1.8: betaine-aldehyde 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 I160 T161 P162 W163 N164 M169 K187 S189 E190 G220 G224 A225 T239 G240 S241 T244 E262 L263 C296 E395 F397 W461 I155 T156 P157 W158 N159 M164 K182 S184 E185 G215 G219 A220 T234 G235 S236 T239 E257 L258 C291 E390 F392 W456
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004029 aldehyde dehydrogenase (NAD+) activity
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:0031402 sodium ion binding
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
GO:0047105 4-trimethylammoniobutyraldehyde dehydrogenase activity
GO:0047107 gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity
Biological Process
GO:0019285 glycine betaine biosynthetic process from choline
GO:0110095 cellular detoxification of aldehyde

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:4i8p, PDBe:4i8p, PDBj:4i8p
PDBsum4i8p
PubMed23408433
UniProtC0P9J6|ADH1A_MAIZE Aminoaldehyde dehydrogenase 1a (Gene Name=AMADH1A)

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