Structure of PDB 1b14 Chain B Binding Site BS01

Receptor Information
>1b14 Chain B (length=254) Species: 7225 (Scaptodrosophila lebanonensis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MDLTNKNVIFVAALGGIGLDTSRELVKRNLKNFVILDRVENPTALAELKA
INPKVNITFHTYDVTVPVAESKKLLKKIFDQLKTVDILINGAGILDDHQI
ERTIAINFTGLVNTTTAILDFWDKRKGGPGGIIANICSVTGFNAIHQVPV
YSASKAAVVSFTNSLAKLAPITGVTAYSINPGITRTPLVHTFNSWLDVEP
RVAELLLSHPTQTSEQCGQNFVKAIEANKNGAIWKLDLGTLEAIEWTKHW
DSHI
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 chain1b14 Chain B Residue 256 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1b14 The catalytic reaction and inhibition mechanism of Drosophila alcohol dehydrogenase: observation of an enzyme-bound NAD-ketone adduct at 1.4 A resolution by X-ray crystallography.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		A12 G15 G16 I17 D37 R38 D63 V64 G91 A92 G93 I106 I136 C137 S138 Y151 K155 P181 T186 L188 V189
Binding residue
(residue number reindexed from 1)		A12 G15 G16 I17 D37 R38 D63 V64 G91 A92 G93 I106 I136 C137 S138 Y151 K155 P181 T186 L188 V189
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) N107 S138 Y151 K155
Catalytic site (residue number reindexed from 1) N107 S138 Y151 K155
Enzyme Commision number 1.1.1.1: alcohol dehydrogenase.
Gene Ontology
Molecular Function
GO:0004022 alcohol dehydrogenase (NAD+) activity
GO:0016491 oxidoreductase activity
GO:0042802 identical protein binding
Biological Process
GO:0006066 alcohol metabolic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1b14, PDBe:1b14, PDBj:1b14
PDBsum1b14
PubMed10366509
UniProtP10807|ADH_DROLE Alcohol dehydrogenase (Gene Name=Adh)

[Back to BioLiP]