Structure of PDB 2jal Chain A Binding Site BS01

Receptor Information
>2jal Chain A (length=436) 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
RAVKVFRETVKDGKIGIVFNNGYFEPASERAVRFMHQFNNYPLFLNPIYR
GDYPELVLEFAREYLPENYKDDMSEIQEKIDFVGLNYYSGHLVKFDPDAK
VSFVERDLPKTAMGWEIVPEGIYWILKKVKEEYNPPEVYITENGAAFDDV
VSEDGRVHDQNRIDYLKAHIGQAWKAIQEGVPLKGYFVWSLLDNFEWAEG
YSKRFGIVYVDYSTQKRIVKDSGYWYSNVVKNNGLE
Ligand information
Ligand IDYLL
InChIInChI=1S/C7H14O6/c8-1-2-3(9)5(11)7(13)6(12)4(2)10/h2-13H,1H2/t2-,3-,4-,5+,6+,7-/m1/s1
InChIKeyQFYQIWDMMSKNFF-NYLBLOMBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(C1O)O)O)O)O)O
OpenEye OEToolkits 1.5.0C(C1[C@H]([C@@H](C([C@H]([C@@H]1O)O)O)O)O)O
CACTVS 3.341OC[CH]1[CH](O)[CH](O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@@H]1[C@@H](O)[C@H](O)[C@@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04OC1C(C(O)C(O)C(O)C1O)CO
FormulaC7 H14 O6
Name(1R,2S,3S,4S,5R,6R)-6-(HYDROXYMETHYL)CYCLOHEXANE-1,2,3,4,5-PENTOL
ChEMBL
DrugBank
ZINC
PDB chain2jal Chain A 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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PDB2jal Structural Basis for Cyclophellitol Inhibition of a Beta-Glucosidase.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Q20 H121 E166 E351 W398 E405 W406 F414
Binding residue
(residue number reindexed from 1)		Q18 H119 E164 E342 W389 E396 W397 F405
Annotation score1
Binding affinityPDBbind-CN: -logKd/Ki=4.82,Ki=15uM
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 N286 Y288 E342
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:2jal, PDBe:2jal, PDBj:2jal
PDBsum2jal
PubMed17252125
UniProtQ08638|BGLA_THEMA Beta-glucosidase A (Gene Name=bglA)

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