Structure of PDB 3wlk Chain X Binding Site BS02

Receptor Information
>3wlk Chain X (length=602) Species: 112509 (Hordeum vulgare subsp. vulgare) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DYVLYKDATKPVEDRVADLLGRMTLAEKIGQMTQIERLVATPDVLRDNFI
GSLLSGGGSVPRKGATAKEWQDMVDGFQKACMSTRLGIPMIYGIDAVHGQ
NNVYGATIFPHNVGLGATRDPYLVKRIGEATALEVRATGIQYAFAPCIAV
CRDPRWGRCYESYSEDRRIVQSMTELIPGLQGDVPKDFTSGMPFVAGKNK
VAACAKHFVGDGGTVDGINENNTIINREGLMNIHMPAYKNAMDKGVSTVM
ISYSSWNGVKMHANQDLVTGYLKDTLKFKGFVISDWEGIDRITTPAGSDY
SYSVKASILAGLDMIMVPNKYQQFISILTGHVNGGVIPMSRIDDAVTRIL
RVKFTMGLFENPYADPAMAEQLGKQEHRDLAREAARKSLVLLKNGKTSTD
APLLPLPKKAPKILVAGSHADNLGYQCGGWTIEWQGDTGRTTVGTTILEA
VKAAVDPSTVVVFAENPDAEFVKSGGFSYAIVAVGEHPYTETKGDNLNLT
IPEPGLSTVQAVCGGVRCATVLISGRPVVVQPLLAASDALVAAWLPGSEG
QGVTDALFGDFGFTGRLPRTWFKSVDQLPMNVGDAHYDPLFRLGYGLTTN
AT
Ligand information
Ligand IDBGC
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-VFUOTHLCSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C(C1C(C(C(C(O1)O)O)O)O)O
CACTVS 3.370OC[C@H]1O[C@@H](O)[C@H](O)[C@@H](O)[C@@H]1O
CACTVS 3.370OC[CH]1O[CH](O)[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.6C([C@@H]1[C@H]([C@@H]([C@H]([C@@H](O1)O)O)O)O)O
ACDLabs 12.01OC1C(O)C(OC(O)C1O)CO
FormulaC6 H12 O6
Namebeta-D-glucopyranose;
beta-D-glucose;
D-glucose;
glucose
ChEMBLCHEMBL1614854
DrugBankDB02379
ZINCZINC000003833800
PDB chain3wlk Chain X Residue 714 [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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PDB3wlk Discovery of processive catalysis by an exo-hydrolase with a pocket-shaped active site.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		D95 R158 K206 H207 M250 Y253 D285 E491
Binding residue
(residue number reindexed from 1)		D95 R158 K206 H207 M250 Y253 D285 E491
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) D285 E491
Catalytic site (residue number reindexed from 1) D285 E491
Enzyme Commision number 3.2.1.21: beta-glucosidase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
Biological Process
GO:0005975 carbohydrate metabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3wlk, PDBe:3wlk, PDBj:3wlk
PDBsum3wlk
PubMed31110237
UniProtQ9XEI3

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