Structure of PDB 5x5u Chain A

Receptor sequence
>5x5uA (length=476) Species: 192 (Azospirillum brasilense) [Search protein sequence]
TYTDTQLLIDGEWVDAASGKTIDVVNPATGKPIGRVAHAGIADLDRALAA
AQSGFEAWRKVPAHERAATMRKAAALVRERADAIAQLMTQEQGKPLTEAR
VEVLSAADIIEWFADEGRRVYGRIVPPRNLGAQQTVVKEPVGPVAAFTPW
NFPVNQVVRKLSAALATGCSFLVKAPEETPASPAALLRAFVDAGVPAGVI
GLVYGDPAEISSYLIPHPVIRKVTFTGSTPVGKQLASLAGLHMKRATMEL
GGHAPVIVAEDADVALAVKAAGGAKFRNAGQVCISPTRFLVHNSIRDEFT
RALVKHAEGLKVGNGLEEGTTLGALANPRRLTAMASVIDNARKVGASIET
GGERIGSEGNFFAPTVIANVPLDADVFNNEPFGPVAAIRGFDKLEEAIAE
ANRLPFGLAGYAFTRSFANVHLLTQRLEVGMLWINQPATPWPEMPFGGVK
DSGYGSEGGPEALEPYLVTKSVTVMA
3D structure
PDB5x5u Structural insights into the production of 3-hydroxypropionic acid by aldehyde dehydrogenase from Azospirillum brasilense.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N155 K178 E253 C287 E384 E461
Catalytic site (residue number reindexed from 1) N151 K174 E249 C283 E380 E457
Enzyme Commision number 1.2.1.24: succinate-semialdehyde dehydrogenase (NAD(+)).
1.2.1.26: 2,5-dioxovalerate 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 P153 P211 A212 S215 G231 S232 V235 R333 R334 E384 F386 P149 P207 A208 S211 G227 S228 V231 R329 R330 E380 F382
BS02 GOL A D19 A20 A21 G23 D15 A16 A17 G19
Gene Ontology
Molecular Function
GO:0004777 succinate-semialdehyde 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:0047533 2,5-dioxovalerate dehydrogenase (NADP+) activity
GO:0070401 NADP+ binding
GO:0070403 NAD+ binding
Biological Process
GO:0009450 gamma-aminobutyric acid catabolic process
GO:0019568 arabinose catabolic process
GO:0019570 L-arabinose catabolic process to 2-oxoglutarate
GO:0051262 protein tetramerization

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Molecular Function
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Biological Process
External links
PDB RCSB:5x5u, PDBe:5x5u, PDBj:5x5u
PDBsum5x5u
PubMed28393833
UniProtQ1JUP4|KGSD1_AZOBR Alpha-ketoglutaric semialdehyde dehydrogenase 1 (Gene Name=araE)

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