Structure of PDB 2zox Chain A Binding Site BS01

Receptor Information
>2zox Chain A (length=466) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MAFPAGFGWAAATAAYQVEGGWDADGKGPCVWDTFTHQGGERVFKNQTGD
VACGSYTLWEEDLKCIKQLGLTHYRFSLSWSRLLPDGTTGFINQKGIDYY
NKIIDDLLKNGVTPIVTLYHFDLPQTLEDQGGWLSEAIIESFDKYAQFCF
STFGDRVKQWITINQANVLSVMSYDLGMFPPGIPHFGTGGYQAAHNLIKA
HARSWHSYDSLFRKKQKGMVSLSLFAVWLEPADPNSVSDQEAAKRAITFH
LDLFAKPIFIDGDYPEVVKSQIASMSQKQGYPSSRLPEFTEEEKKMIKGT
ADFFAVQYYTTRLIKYQENKKGELGILQDAEIEFFPDPSWKNVDWIYVVP
WGVCKLLKYIKDTYNNPVIYITENGFPQSDPAPLDDTQRWEYFRQTFQEL
FKAIQLDKVNLQVYCAWSLLDNFEWNQGYSSRFGLFHVDFEDPARPRVPY
TSAKEYAKIIRNNGLE
Ligand information
Ligand IDGLC
InChIInChI=1S/C6H12O6/c7-1-2-3(8)4(9)5(10)6(11)12-2/h2-11H,1H2/t2-,3-,4+,5-,6+/m1/s1
InChIKeyWQZGKKKJIJFFOK-DVKNGEFBSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(C1C(C(C(C(O1)O)O)O)O)O
OpenEye OEToolkits 1.5.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O)O
CACTVS 3.341OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
CACTVS 3.341OC[C@H]1O[C@H](O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namealpha-D-glucopyranose;
alpha-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL423707
DrugBank
ZINCZINC000003861213
PDB chain2zox Chain A Residue 470 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2zox Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Q17 H120 N164 Y309 E373 W417 E424 W425 F433
Binding residue
(residue number reindexed from 1)		Q17 H120 N164 Y309 E373 W417 E424 W425 F433
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) R75 H120 Q165 V168 Q307 Y309 E373
Catalytic site (residue number reindexed from 1) R75 H120 Q165 V168 Q307 Y309 E373
Enzyme Commision number 3.2.1.21: beta-glucosidase.
3.2.1.45: glucosylceramidase.
3.2.1.46: galactosylceramidase.
Gene Ontology
Molecular Function
GO:0004336 galactosylceramidase activity
GO:0004348 glucosylceramidase activity
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004565 beta-galactosidase activity
GO:0005515 protein binding
GO:0008422 beta-glucosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0017042 glycosylceramidase activity
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006629 lipid metabolic process
GO:0006680 glucosylceramide catabolic process
GO:0006683 galactosylceramide catabolic process
GO:0009313 oligosaccharide catabolic process
GO:0016139 glycoside catabolic process
GO:0046477 glycosylceramide catabolic process
GO:0046479 glycosphingolipid catabolic process
GO:0050821 protein stabilization
GO:1901805 beta-glucoside catabolic process
GO:1903017 positive regulation of exo-alpha-sialidase activity
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:1902494 catalytic complex

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2zox, PDBe:2zox, PDBj:2zox
PDBsum2zox
PubMed18662675
UniProtQ9H227|GBA3_HUMAN Cytosolic beta-glucosidase (Gene Name=GBA3)

[Back to BioLiP]