Structure of PDB 1exp Chain A Binding Site BS01

Receptor Information
>1exp Chain A (length=312) Species: 1708 (Cellulomonas fimi) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATTLKEAADGAGRDFGFALDPNRLSEAQYKAIADSEFNLVVAENAMKWDA
TEPSQNSFSFGAGDRVASYAADTGKELYGHTLVWHSQLPDWAKNLNGSAF
ESAMVNHVTKVADHFEGKVASWDVVNEAFADGGGRRQDSAFQQKLGNGYI
ETAFRAARAADPTAKLCINDYNVEGINAKSNSLYDLVKDFKARGVPLDCV
GFQSHLIVGQVPGDFRQNLQRFADLGVDVRITELDIRMRTPSDATKLATQ
AADYKKVVQACMQVTRCQGVTVWGITDKYSWVPDVFPGEGAALVWDASYA
KKPAYAAVMEAF
Ligand information
Ligand IDG2F
InChIInChI=1S/C6H11FO5/c7-3-5(10)4(9)2(1-8)12-6(3)11/h2-6,8-11H,1H2/t2-,3-,4-,5-,6+/m1/s1
InChIKeyZCXUVYAZINUVJD-UKFBFLRUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.0C(C1C(C(C(C(O1)O)F)O)O)O
CACTVS 3.370OC[CH]1O[CH](O)[CH](F)[CH](O)[CH]1O
OpenEye OEToolkits 1.7.0C([C@@H]1[C@H]([C@@H]([C@H]([C@H](O1)O)F)O)O)O
CACTVS 3.370OC[C@H]1O[C@H](O)[C@H](F)[C@@H](O)[C@@H]1O
ACDLabs 12.01FC1C(O)C(O)C(OC1O)CO
FormulaC6 H11 F O5
Name2-deoxy-2-fluoro-alpha-D-glucopyranose;
2-deoxy-2-fluoro-alpha-D-glucose;
2-deoxy-2-fluoro-D-glucose;
2-deoxy-2-fluoro-glucose
ChEMBLCHEMBL1086863
DrugBankDB04282
ZINCZINC000003809846
PDB chain1exp Chain B Residue 1 [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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PDB1exp Crystallographic observation of a covalent catalytic intermediate in a beta-glycosidase.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		K47 H80 W84 Q203 H205 E233 W273 W281
Binding residue
(residue number reindexed from 1)		K47 H80 W84 Q203 H205 E233 W273 W281
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E127 N169 H205 E233 D235
Catalytic site (residue number reindexed from 1) E127 N169 H205 E233 D235
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-reducing end).
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1exp, PDBe:1exp, PDBj:1exp
PDBsum1exp
PubMed8564541
UniProtP07986|GUX_CELFI Exoglucanase/xylanase (Gene Name=cex)

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