Structure of PDB 2zox Chain A Binding Site BS02

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 IDPNG
InChIInChI=1S/C12H15NO8/c14-5-8-9(15)10(16)11(17)12(21-8)20-7-3-1-6(2-4-7)13(18)19/h1-4,8-12,14-17H,5H2/t8-,9-,10+,11-,12+/m1/s1
InChIKeyIFBHRQDFSNCLOZ-ZIQFBCGOSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC[C@H]1O[C@H](Oc2ccc(cc2)[N+]([O-])=O)[C@H](O)[C@@H](O)[C@@H]1O
ACDLabs 10.04[O-][N+](=O)c2ccc(OC1OC(C(O)C(O)C1O)CO)cc2
OpenEye OEToolkits 1.5.0c1cc(ccc1[N+](=O)[O-])O[C@@H]2[C@@H]([C@H]([C@@H]([C@H](O2)CO)O)O)O
OpenEye OEToolkits 1.5.0c1cc(ccc1[N+](=O)[O-])OC2C(C(C(C(O2)CO)O)O)O
CACTVS 3.341OC[CH]1O[CH](Oc2ccc(cc2)[N+]([O-])=O)[CH](O)[CH](O)[CH]1O
FormulaC12 H15 N O8
Name4-nitrophenyl alpha-D-glucopyranoside;
4'-NITROPHENYL-ALPHA-D-GLUCOPYRANOSIDE;
4-nitrophenyl alpha-D-glucoside;
4-nitrophenyl D-glucoside;
4-nitrophenyl glucoside
ChEMBLCHEMBL1235365
DrugBank
ZINCZINC000004282228
PDB chain2zox Chain A Residue 471 [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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PDB2zox Crystal structure of the covalent intermediate of human cytosolic beta-glucosidase
Resolution1.9 Å
Binding residue
(original residue number in PDB)		S274 M275 K278 E318 K320 G322 E331
Binding residue
(residue number reindexed from 1)		S274 M275 K278 E318 K320 G322 E331
Annotation score1
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

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

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