Structure of PDB 2fgl Chain A Binding Site BS05

Receptor Information
>2fgl Chain A (length=354) Species: 65673 (Bacillus sp. NG-27) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VQPFAWQVASLADRYEESFDIGAAVEPHQLNGRQGKVLKHHYNSIVAENA
MKPISLQPEEGVFTWDGADAIVEFARKNNMNLRFHTLVWHNQVPDWFFLD
EEGNPMVEETNEAKRQANKELLLERLETHIKTVVERYKDDVTAWDVVNEV
VDDGTPNERGLRESVWYQITGDEYIRVAFETARKYAGEDAKLFINDYNTE
VTPKRDHLYNLVQDLLADGVPIDGVGHQAHIQIDWPTIDEIRTSMEMFAG
LGLDNQVTELDVSLYGWPPRPAFPTYDAIPQERFQAQADRYNQLFELYEE
LDADLSSVTFWGIADNHTWLDDRAREYNDGVGKDAPFVFDPNYRVKPAFW
RIID
Ligand information
Ligand IDXYS
InChIInChI=1S/C5H10O5/c6-2-1-10-5(9)4(8)3(2)7/h2-9H,1H2/t2-,3+,4-,5+/m1/s1
InChIKeySRBFZHDQGSBBOR-LECHCGJUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C1C(C(C(C(O1)O)O)O)O
CACTVS 3.341O[CH]1CO[CH](O)[CH](O)[CH]1O
OpenEye OEToolkits 1.5.0C1[C@H]([C@@H]([C@H]([C@H](O1)O)O)O)O
CACTVS 3.341O[C@@H]1CO[C@H](O)[C@H](O)[C@H]1O
ACDLabs 10.04OC1C(O)COC(O)C1O
FormulaC5 H10 O5
Namealpha-D-xylopyranose;
alpha-D-xylose;
D-xylose;
xylose;
XYLOPYRANOSE
ChEMBL
DrugBankDB03389
ZINCZINC000001529214
PDB chain2fgl Chain A Residue 704 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fgl Crystal structures of native and xylosaccharide-bound alkali thermostable xylanase from an alkalophilic Bacillus sp. NG-27: structural insights into alkalophilicity and implications for adaptation to polyextreme conditions.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		N198 Q232 W235 W267
Binding residue
(residue number reindexed from 1)		N198 Q232 W235 W267
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) E149 N195 H230 E259 D261
Catalytic site (residue number reindexed from 1) E149 N195 H230 E259 D261
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0031176 endo-1,4-beta-xylanase activity
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0045493 xylan catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2fgl, PDBe:2fgl, PDBj:2fgl
PDBsum2fgl
PubMed16823036
UniProtO30700

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