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8QY2

Xylanase from Bacillus circulans mutant E78Q/F125A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031176molecular_functionendo-1,4-beta-xylanase activity
A0045493biological_processxylan catabolic process
Functional Information from PROSITE/UniProt
site_idPS00777
Number of Residues12
DetailsGH11_2 Glycosyl hydrolases family 11 (GH11) active site signature 2. MatEGYQSSGsS
ChainResidueDetails
AMET169-SER180

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10062, ECO:0000269|PubMed:8019418
ChainResidueDetails
AGLN78

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU10063, ECO:0000269|PubMed:8019418
ChainResidueDetails
AGLU172

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 432
ChainResidueDetails
AASN35modifies pKa
ATYR69electrostatic destabiliser
AGLN78covalent catalysis, proton shuttle (general acid/base)
ATYR80modifies pKa
AGLU172proton shuttle (general acid/base)

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PDB entries from 2025-06-18

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