Structure of PDB 5u0m Chain B Binding Site BS01

Receptor Information
>5u0m Chain B (length=487) Species: 351348 (Marinobacter nauticus VT8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LTGNVYIDGLWLPGHGAPFESVQPVTGETVWDGNAASLEDVDAAVREARK
AFLAWRRKSLAERQAVIEAFGELLEANKEELAHQIGLETGKPLWESRTEV
AAMMGKIPISVKAYNERTGHTESDVAGGHAVLRHRPHGVVAVFGPYNFPG
HLPNGHIVPALLAGNTVVFKPSELTPGVAELTVRLWEKAGLPDGVINLVQ
GGSDTGKCLARHSLIDGLFFTGSSTVGHLLHEQFGGQPEKILALEMGGNN
PLIVQNVSDLDGAVHHALQSAFLSAGQRCTCARRLLVPKGKKGDEFLARL
VEVAARITVAEFDADPQPFMGSVISAEAANQLLKAQAAMLEKGATSLLEM
KQLKPDTGLLSPGIVDATGIELEDQEFFGPLLTVYRYKGFDEALELANNT
RYGLSAGILSDDRKLYNRLVEEVRAGIVNWNRPLTGASSAAPFGGVGASG
NHRPSAYYAADYCAWPMASLEAGKSELPDSLAPGLNF
Ligand information
Ligand IDNAD
InChIInChI=1S/C21H27N7O14P2/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(32)14(30)11(41-21)6-39-44(36,37)42-43(34,35)38-5-10-13(29)15(31)20(40-10)27-3-1-2-9(4-27)18(23)33/h1-4,7-8,10-11,13-16,20-21,29-32H,5-6H2,(H5-,22,23,24,25,33,34,35,36,37)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1
InChIKeyBAWFJGJZGIEFAR-NNYOXOHSSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
CACTVS 3.341NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)O)O)O)O)C(=O)N
FormulaC21 H27 N7 O14 P2
NameNICOTINAMIDE-ADENINE-DINUCLEOTIDE
ChEMBLCHEMBL1234613
DrugBankDB14128
ZINC
PDB chain5u0m Chain B Residue 503 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5u0m Five Fatty Aldehyde Dehydrogenase Enzymes from Marinobacter and Acinetobacter spp. and Structural Insights into the Aldehyde Binding Pocket.
Resolution3.075 Å
Binding residue
(original residue number in PDB)		F146 G147 P148 Y149 N150 L155 K173 S175 E176 G209 G225 S226 E248 M249 C282 E379 F381
Binding residue
(residue number reindexed from 1)		F143 G144 P145 Y146 N147 L152 K170 S172 E173 G206 G222 S223 E245 M246 C279 E376 F378
Annotation score4
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.
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)

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