Structure of PDB 4dyd Chain A Binding Site BS01

Receptor Information
>4dyd Chain A (length=283) Species: 202950 (Acinetobacter baylyi) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MTGITNVTVLGTGVLGSQIAFQTAFHGFAVTAYDINTDALDAAKKRFEGL
AAVYEKEVAGAADGAAQKALGGIRYSDDLAQAVKDADLVIEAVPESLDLK
RDIYTKLGELAPAKTIFATNSSTLLPSDLVGYTGRGDKFLALHFANHVWV
NNTAEVMGTTKTDPEVYQQVVEFASAIGMVPIELKKEKAGYVLNSLLVPL
LDAAAELLVDGIADPETIDKTWRIGTGAPKGPFEIFDIVGLTTAYNISSV
SGPKQREFAAYLKENYIDKGKLGLATGEGFYRY
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 chain4dyd Chain A Residue 301 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4dyd Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase
Resolution1.95 Å
Binding residue
(original residue number in PDB)		G11 T12 G13 V14 L15 D34 I35 V93 P94 E95 L99 K100 N120 S122 H143
Binding residue
(residue number reindexed from 1)		G11 T12 G13 V14 L15 D34 I35 V93 P94 E95 L99 K100 N120 S122 H143
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) S122 H143 E155 N194
Catalytic site (residue number reindexed from 1) S122 H143 E155 N194
Enzyme Commision number 1.1.1.35: 3-hydroxyacyl-CoA dehydrogenase.
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003857 3-hydroxyacyl-CoA dehydrogenase activity
GO:0016491 oxidoreductase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0070403 NAD+ binding
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006635 fatty acid beta-oxidation
GO:0009056 catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4dyd, PDBe:4dyd, PDBj:4dyd
PDBsum4dyd
PubMed23073461
UniProtB1P3E1

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