Structure of PDB 5u0m Chain A Binding Site BS01

Receptor Information
>5u0m Chain A (length=488) Species: 351348 (Marinobacter nauticus VT8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NLTGNVYIDGLWLPGHGAPFESVQPVTGETVWDGNAASLEDVDAAVREAR
KAFLAWRRKSLAERQAVIEAFGELLEANKEELAHQIGLETGKPLWESRTE
VAAMMGKIPISVKAYNERTGHTESDVAGGHAVLRHRPHGVVAVFGPYNFP
GHLPNGHIVPALLAGNTVVFKPSELTPGVAELTVRLWEKAGLPDGVINLV
QGGSDTGKCLARHSLIDGLFFTGSSTVGHLLHEQFGGQPEKILALEMGGN
NPLIVQNVSDLDGAVHHALQSAFLSAGQRCTCARRLLVPKGKKGDEFLAR
LVEVAARITVAEFDADPQPFMGSVISAEAANQLLKAQAAMLEKGATSLLE
MKQLKPDTGLLSPGIVDATGIELEDQEFFGPLLTVYRYKGFDEALELANN
TRYGLSAGILSDDRKLYNRLVEEVRAGIVNWNRPLTGASSAAPFGGVGAS
GNHRPSAYYAADYCAWPMASLEAGKSELPDSLAPGLNF
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 A Residue 504 [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 Y149 N150 K173 S175 E176 G209 T224 G225 S226 V229 E248 M249 G250 C282 E379 F381
Binding residue
(residue number reindexed from 1)		F144 Y147 N148 K171 S173 E174 G207 T222 G223 S224 V227 E246 M247 G248 C280 E377 F379
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N150 K173 E248 C282 E379 P457
Catalytic site (residue number reindexed from 1) N148 K171 E246 C280 E377 P455
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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