Structure of PDB 1oim Chain B Binding Site BS01

Receptor Information
>1oim Chain B (length=444) Species: 2336 (Thermotoga maritima) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SNVKKFPEGFLWGVATASYQIEGSPLADGAGMSIWHTFSHTPGNVKNGDT
GDVACDHYNRWKEDIEIIEKLGVKAYRFSISWPRILPEGTGRVNQKGLDF
YNRIIDTLLEKGITPFVTIYHWDLPFALQLKGGWANREIADWFAEYSRVL
FENFGDRVKNWITLNEPWVVAIVGHLYGVHAPGMRDIYVAFRAVHNLLRA
HARAVKVFRETVDGKIGIVFNNGYFEPASEKEEDIRAVRFMHQFNNYPLF
LNPIYRGDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVK
FDPDAAKVSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITEN
GAAFDDVVSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLD
NFEWAEGYSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLED
Ligand information
Ligand IDNOJ
InChIInChI=1S/C6H13NO4/c8-2-3-5(10)6(11)4(9)1-7-3/h3-11H,1-2H2/t3-,4+,5-,6-/m1/s1
InChIKeyLXBIFEVIBLOUGU-JGWLITMVSA-N
SMILES
SoftwareSMILES
ACDLabs 12.01OC1C(NCC(O)C1O)CO
OpenEye OEToolkits 1.7.0C1C(C(C(C(N1)CO)O)O)O
OpenEye OEToolkits 1.7.0C1[C@@H]([C@H]([C@@H]([C@H](N1)CO)O)O)O
CACTVS 3.370OC[CH]1NC[CH](O)[CH](O)[CH]1O
CACTVS 3.370OC[C@H]1NC[C@H](O)[C@@H](O)[C@@H]1O
FormulaC6 H13 N O4
Name1-DEOXYNOJIRIMYCIN;
MORANOLINE
ChEMBLCHEMBL307429
DrugBankDB03206
ZINCZINC000003794714
PDB chain1oim Chain B Residue 1447 [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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PDB1oim Iminosugar Glycosidase Inhibitors: Structural and Thermodynamic Dissection of the Binding of Isofagomine and 1-Deoxynojirimycin to Beta-Glucosidases
Resolution2.15 Å
Binding residue
(original residue number in PDB)		Q20 H121 N165 E166 Y295 W324 E351 W398 E405
Binding residue
(residue number reindexed from 1)		Q20 H121 N165 E166 Y294 W322 E349 W396 E403
Annotation score1
Binding affinityMOAD: Ka=210000M^-1
Enzymatic activity
Catalytic site (original residue number in PDB) R77 H121 E166 V169 N293 Y295 E351
Catalytic site (residue number reindexed from 1) R77 H121 E166 V169 N292 Y294 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:1oim, PDBe:1oim, PDBj:1oim
PDBsum1oim
PubMed14624580
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

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