Structure of PDB 1rwb Chain A Binding Site BS01

Receptor Information
>1rwb Chain A (length=261) Species: 1404 (Priestia megaterium) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MYKDLEGKVVVITGSSTGLGKSMAIRFATEKAKVVVNYRSKEDEANSVLE
EIKKVGGEAIAVKGDVTVESDVINLVQSAIKEFGKLDVMINNAGLENPVS
SHEMSLSDWNKVIDTNLTGAFLGSREAIKYFVENDIKGTVINMSSVHEKI
PWPLFVHYAASKGGMKLMTKTLALEYAPKGIRVNNIGPGAINTPINAEKF
ADPEQRADVESMIPMGYIGEPEEIAAVAAWLASSEASYVTGITLFADGGM
TLYPSFQAGRG
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 chain1rwb Chain A Residue 601 [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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PDB1rwb Cooperative effect of two surface amino acid mutations (Q252L and E170K) in glucose dehydrogenase from Bacillus megaterium IWG3 on stabilization of its oligomeric state.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		G14 T17 G18 L19 R39 D65 V66 N92 A93 G94 T115 M143 S144 S145 Y158 K162 P188 G189 I191 T193
Binding residue
(residue number reindexed from 1)		G14 T17 G18 L19 R39 D65 V66 N92 A93 G94 T115 M143 S144 S145 Y158 K162 P188 G189 I191 T193
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) G18 S145 Y158 K162
Catalytic site (residue number reindexed from 1) G18 S145 Y158 K162
Enzyme Commision number 1.1.1.47: glucose 1-dehydrogenase [NAD(P)(+)].
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0047934 glucose 1-dehydrogenase (NAD+) activity
GO:0047935 glucose 1-dehydrogenase (NADP+) activity
GO:0047936 glucose 1-dehydrogenase [NAD(P)+] activity
Biological Process
GO:0030435 sporulation resulting in formation of a cellular spore

View graph for
Molecular Function
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Biological Process
External links
PDB RCSB:1rwb, PDBe:1rwb, PDBj:1rwb
PDBsum1rwb
PubMed15933031
UniProtP40288|DHG_PRIMG Glucose 1-dehydrogenase

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