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6RK2

Complex structure of virulence factor SghA mutant with its substrate SAG

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008422molecular_functionbeta-glucosidase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030245biological_processcellulose catabolic process
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008422molecular_functionbeta-glucosidase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030245biological_processcellulose catabolic process
Functional Information from PROSITE/UniProt
site_idPS00572
Number of Residues9
DetailsGLYCOSYL_HYDROL_F1_1 Glycosyl hydrolases family 1 active site. CYITENGAC
ChainResidueDetails
ACYS363-CYS371

site_idPS00653
Number of Residues15
DetailsGLYCOSYL_HYDROL_F1_2 Glycosyl hydrolases family 1 N-terminal signature. FlFGvAtASFQiEgA
ChainResidueDetails
APHE23-ALA37

238582

PDB entries from 2025-07-09

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