Structure of PDB 5u0m Chain B

Receptor sequence
>5u0mB (length=487) Species: 351348 (Marinobacter nauticus VT8) [Search protein sequence]
LTGNVYIDGLWLPGHGAPFESVQPVTGETVWDGNAASLEDVDAAVREARK
AFLAWRRKSLAERQAVIEAFGELLEANKEELAHQIGLETGKPLWESRTEV
AAMMGKIPISVKAYNERTGHTESDVAGGHAVLRHRPHGVVAVFGPYNFPG
HLPNGHIVPALLAGNTVVFKPSELTPGVAELTVRLWEKAGLPDGVINLVQ
GGSDTGKCLARHSLIDGLFFTGSSTVGHLLHEQFGGQPEKILALEMGGNN
PLIVQNVSDLDGAVHHALQSAFLSAGQRCTCARRLLVPKGKKGDEFLARL
VEVAARITVAEFDADPQPFMGSVISAEAANQLLKAQAAMLEKGATSLLEM
KQLKPDTGLLSPGIVDATGIELEDQEFFGPLLTVYRYKGFDEALELANNT
RYGLSAGILSDDRKLYNRLVEEVRAGIVNWNRPLTGASSAAPFGGVGASG
NHRPSAYYAADYCAWPMASLEAGKSELPDSLAPGLNF
3D structure
PDB5u0m Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket.
ChainB
Resolution3.075 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) N150 K173 E248 C282 E379 P457
Catalytic site (residue number reindexed from 1) N147 K170 E245 C279 E376 P454
Enzyme Commision number 1.2.1.71: succinylglutamate-semialdehyde 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 B F146 G147 P148 Y149 N150 L155 K173 S175 E176 G209 G225 S226 E248 M249 C282 E379 F381 F143 G144 P145 Y146 N147 L152 K170 S172 E173 G206 G222 S223 E245 M246 C279 E376 F378
Gene Ontology
Molecular Function
GO:0004029 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:0043824 succinylglutamate-semialdehyde dehydrogenase activity
Biological Process
GO:0006525 arginine metabolic process
GO:0006527 arginine catabolic process
GO:0019544 arginine catabolic process to glutamate
GO:0019545 arginine catabolic process to succinate

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5u0m, PDBe:5u0m, PDBj:5u0m
PDBsum5u0m
PubMed28389542
UniProtA1U5W8|ASTD_MARN8 N-succinylglutamate 5-semialdehyde dehydrogenase (Gene Name=astD)

[Back to BioLiP]