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1EQP

EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0006696biological_processergosterol biosynthetic process
A0007155biological_processcell adhesion
A0008152biological_processmetabolic process
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
A0050839molecular_functioncell adhesion molecule binding
A0071555biological_processcell wall organization
A0071704biological_processorganic substance metabolic process
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
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:O85465
ChainResidueDetails
AGLU192

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:9013549
ChainResidueDetails
AGLU292

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:20875088
ChainResidueDetails
ATYR29
AGLU27
AGLU192
ATYR255
AGLU262

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 831
ChainResidueDetails
AGLU192activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
AGLU292covalently attached, nucleofuge, nucleophile

218500

PDB entries from 2024-04-17

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