Structure of PDB 1geg Chain F Binding Site BS02

Receptor Information
>1geg Chain F (length=255) Species: 573 (Klebsiella pneumoniae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KKVALVTGAGQGIGKAIALRLVKDGFAVAIADYNDATAKAVASEINQAGG
HAVAVKVDVSDRDQVFAAVEQARKTLGGFDVIVNNAGVAPSTPIESITPE
IVDKVYNINVKGVIWGIQAAVEAFKKEGHGGKIINACSQAGHVGNPELAV
YSSSKFAVRGLTQTAARDLAPLGITVNGYCPGIVKTPMWAEIDRQVSEAA
GKPLGYGTAEFAKRITLGRLSEPEDVAACVSYLASPDSDYMTGQSLLIDG
GMVFN
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 chain1geg Chain F Residue 308 [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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PDB1geg Crystal structure of meso-2,3-butanediol dehydrogenase in a complex with NAD+ and inhibitor mercaptoethanol at 1.7 A resolution for understanding of chiral substrate recognition mechanisms.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		G9 Q12 I14 D33 Y34 V58 D59 V60 N86 A87 I109 S139 Y152 K156 P182 V185 T187 M189
Binding residue
(residue number reindexed from 1)		G8 Q11 I13 D32 Y33 V57 D58 V59 N85 A86 I108 S138 Y151 K155 P181 V184 T186 M188
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) G13 S139 Y152 K156 V197
Catalytic site (residue number reindexed from 1) G12 S138 Y151 K155 V196
Enzyme Commision number 1.1.1.304: diacetyl reductase [(S)-acetoin forming].
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0019152 acetoin dehydrogenase (NAD+) activity
GO:0052588 diacetyl reductase ((S)-acetoin forming) (NAD+) activity
Biological Process
GO:0045150 acetoin catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1geg, PDBe:1geg, PDBj:1geg
PDBsum1geg
PubMed11173520
UniProtQ48436|BUDC_KLEPN Diacetyl reductase [(S)-acetoin forming] (Gene Name=budC)

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