Structure of PDB 2wc4 Chain D Binding Site BS01

Receptor Information
>2wc4 Chain D (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 IDAMF
InChIInChI=1S/C15H28N2O4S/c1-2-3-4-5-6-7-8-16-15-17-10(9-22-15)11(18)12(19)13(20)14(17)21/h10-14,18-21H,2-9H2,1H3/b16-15-/t10-,11-,12+,13-,14+/m1/s1
InChIKeyHXWFEIXEWVGTGU-KRIYVDMXSA-N
SMILES
SoftwareSMILES
CACTVS 3.352CCCCCCCCN=C1SC[CH]2[CH](O)[CH](O)[CH](O)[CH](O)N12
ACDLabs 10.04N(=C1\SCC2N1C(O)C(O)C(O)C2O)\CCCCCCCC
OpenEye OEToolkits 1.6.1CCCCCCCCN=C1N2[C@H](CS1)[C@H]([C@@H]([C@H]([C@@H]2O)O)O)O
OpenEye OEToolkits 1.6.1CCCCCCCCN=C1N2C(CS1)C(C(C(C2O)O)O)O
CACTVS 3.352CCCCCCCCN=C1SC[C@@H]2[C@@H](O)[C@H](O)[C@@H](O)[C@H](O)N12
FormulaC15 H28 N2 O4 S
Name(3Z,5S,6R,7S,8R,8aS)-3-(octylimino)hexahydro[1,3]thiazolo[3,4-a]pyridine-5,6,7,8-tetrol
ChEMBL
DrugBankDB07370
ZINCZINC000053683014
PDB chain2wc4 Chain D Residue 1446 [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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PDB2wc4 Glycosidase Inhibition by Ring-Modified Castanospermine Analogues: Tackling Enzyme Selectivity by Inhibitor Tailoring.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		Q20 H121 N165 E166 Y295 H298 W324 E351 W398 E405 W406 F414
Binding residue
(residue number reindexed from 1)		Q18 H119 N163 E164 Y293 H296 W322 E349 W396 E403 W404 F412
Annotation score1
Binding affinityMOAD: Kd=5.1uM
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:2wc4, PDBe:2wc4, PDBj:2wc4
PDBsum2wc4
PubMed19532990
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

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