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1UHV

Crystal structure of beta-D-xylosidase from Thermoanaerobacterium saccharolyticum, a family 39 glycoside hydrolase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008152biological_processmetabolic process
A0009044molecular_functionxylan 1,4-beta-xylosidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0045493biological_processxylan catabolic process
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008152biological_processmetabolic process
B0009044molecular_functionxylan 1,4-beta-xylosidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0045493biological_processxylan catabolic process
C0000272biological_processpolysaccharide catabolic process
C0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
C0005975biological_processcarbohydrate metabolic process
C0008152biological_processmetabolic process
C0009044molecular_functionxylan 1,4-beta-xylosidase activity
C0016787molecular_functionhydrolase activity
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0045493biological_processxylan catabolic process
D0000272biological_processpolysaccharide catabolic process
D0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
D0005975biological_processcarbohydrate metabolic process
D0008152biological_processmetabolic process
D0009044molecular_functionxylan 1,4-beta-xylosidase activity
D0016787molecular_functionhydrolase activity
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0045493biological_processxylan catabolic process
Functional Information from PROSITE/UniProt
site_idPS01027
Number of Residues10
DetailsGLYCOSYL_HYDROL_F39 Glycosyl hydrolases family 39 active site. WpFEiWNEPN
ChainResidueDetails
ATRP153-ASN162

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10068
ChainResidueDetails
AGLU160
BGLU160
CGLU160
DGLU160

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9761746
ChainResidueDetails
AGLU277
BGLU277
CGLU277
DGLU277

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PDB entries from 2024-04-17

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