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5Y3X

Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0031176molecular_functionendo-1,4-beta-xylanase activity
B0045493biological_processxylan catabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0031176molecular_functionendo-1,4-beta-xylanase activity
C0045493biological_processxylan catabolic process
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0031176molecular_functionendo-1,4-beta-xylanase activity
D0045493biological_processxylan catabolic process
E0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
E0005975biological_processcarbohydrate metabolic process
E0031176molecular_functionendo-1,4-beta-xylanase activity
E0045493biological_processxylan catabolic process
F0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
F0005975biological_processcarbohydrate metabolic process
F0031176molecular_functionendo-1,4-beta-xylanase activity
F0045493biological_processxylan catabolic process
Functional Information from PROSITE/UniProt
site_idPS00591
Number of Residues11
DetailsGH10_1 Glycosyl hydrolases family 10 (GH10) active site. GLEIqITELDM
ChainResidueDetails
AGLY240-MET250

257179

PDB entries from 2026-07-29

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