Structure of PDB 2vrj Chain B Binding Site BS01

Receptor Information
>2vrj Chain B (length=443) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDTGD
VACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDFYN
RIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVLFE
NFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRAHA
RAVKVFRETVKDGKIGIVFNNGYFEPASEKEEDIRAVRFMHQFNNYPLFL
NPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKF
DPDAPAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITEN
GAAFDDVVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLD
NFEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLE
Ligand information
Ligand IDNCW
InChIInChI=1S/C15H28N2O4S/c1-2-3-4-5-6-7-8-16-15(22)17-10-9-21-14(17)13(20)12(19)11(10)18/h10-14,18-20H,2-9H2,1H3,(H,16,22)/t10-,11+,12-,13+,14+/m0/s1
InChIKeyLFSNQOFOMJLHIW-MEBFFEOJSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CCCCCCCCNC(=S)N1[C@H]2CO[C@@H]1[C@H](O)[C@@H](O)[C@@H]2O
OpenEye OEToolkits 1.5.0CCCCCCCCNC(=S)N1[C@H]2CO[C@@H]1[C@@H]([C@H]([C@@H]2O)O)O
CACTVS 3.341CCCCCCCCNC(=S)N1[CH]2CO[CH]1[CH](O)[CH](O)[CH]2O
OpenEye OEToolkits 1.5.0CCCCCCCCNC(=S)N1C2COC1C(C(C2O)O)O
ACDLabs 10.04S=C(N2C1C(O)C(O)C(O)C2OC1)NCCCCCCCC
FormulaC15 H28 N2 O4 S
Name(1S,2R,3S,4R,5R)-2,3,4-trihydroxy-N-octyl-6-oxa-8-azabicyclo[3.2.1]octane-8-carbothioamide
ChEMBL
DrugBankDB08260
ZINCZINC000053683045
PDB chain2vrj Chain B Residue 1446 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2vrj Molecular Basis for Beta-Glucosidase Inhibition by Ring-Modified Calystegine Analogues.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Q20 E166 Y177 Y295 E351 W398 E405 W406
Binding residue
(residue number reindexed from 1)		Q18 E164 Y175 Y293 E349 W396 E403 W404
Annotation score1
Binding affinityMOAD: Kd=0.5uM
Enzymatic activity
Catalytic site (original residue number in PDB) R77 H121 E166 V169 N293 Y295 E351
Catalytic site (residue number reindexed from 1) R75 H119 E164 V167 N291 Y293 E349
Enzyme Commision number 3.2.1.21: beta-glucosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0030245 cellulose catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2vrj, PDBe:2vrj, PDBj:2vrj
PDBsum2vrj
PubMed18833549
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

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