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4M80

The structure of E292S glycosynthase variant of exo-1,3-beta-glucanase from Candida albicans at 1.85A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0007155biological_processcell adhesion
A0009251biological_processglucan catabolic process
A0009986cellular_componentcell surface
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031505biological_processfungal-type cell wall organization
A0031589biological_processcell-substrate adhesion
A0044011biological_processsingle-species biofilm formation on inanimate substrate
A0044042biological_processglucan metabolic process
A0044407biological_processsingle-species biofilm formation in or on host organism
A0044650biological_processadhesion of symbiont to host cell
A0050839molecular_functioncell adhesion molecule binding
A0071555biological_processcell wall organization
A1903561cellular_componentextracellular vesicle
Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. IGIELLNEPL
ChainResidueDetails
AILE185-LEU194

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"O85465","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9013549","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20875088","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 831
ChainResidueDetails
AGLU192activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
ASER292covalently attached, nucleofuge, nucleophile

239149

PDB entries from 2025-07-23

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