Structure of PDB 1up6 Chain A Binding Site BS01

Receptor Information
>1up6 Chain A (length=413) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMRIAVIGGGSSYTPELVKGLLDISEDVRIDEVIFYDIDEEKQKIVVDFV
KRLVKDRFKVLISDTFEGAVVDAKYVIFQFRPGGLKGRENDEGIPLKYGL
IGQETTGVGGFSAALRAFPIVEEYVDTVRKTSNATIVNFTNPSGHITEFV
RNYLEYEKFIGLCNVPINFIREIAEMFSARLEDVFLKYYGLNHLSFIEKV
FVKGEDVTEKVFENLKLKLPDEDFPTWFYDSVRLIVNPYLRYYLMEKKMF
KKISTHELRAREVMKIEKELFEKYRTAVEIPEELTKRGGSMYSTAAAHLI
RDLETDEGKIHIVNTRNNGSIENLPDDYVLEIPCYVRSGRVHTLSQGKGD
HFALSFIHAVKMYERLTIEAYLKRSKKLALKALLSHPLGPDVEDAKDLLE
EILEANREYVKLG
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 chain1up6 Chain A Residue 1416 [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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PDB1up6 An Unusual Mechanism of Glycoside Hydrolysis Involving Redox and Elimination Steps by a Family 4 Beta-Glycosidase from Thermotoga Maritima.
Resolution2.55 Å
Binding residue
(original residue number in PDB)		S10 Y12 D36 I37 K41 Q78 F79 R80 Y123 F138 N140 C162 N163 E269
Binding residue
(residue number reindexed from 1)		S11 Y13 D37 I38 K42 Q79 F80 R81 Y124 F139 N141 C163 N164 E267
Annotation score1
Enzymatic activity
Enzyme Commision number 3.2.1.86: 6-phospho-beta-glucosidase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008706 6-phospho-beta-glucosidase activity
GO:0016616 oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1up6, PDBe:1up6, PDBj:1up6
PDBsum1up6
PubMed15237973
UniProtQ9X108|BGLT_THEMA 6-phospho-beta-glucosidase BglT (Gene Name=bglT)

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