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1H4P

Crystal structure of exo-1,3-beta glucanse from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0000324cellular_componentfungal-type vacuole
A0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0009251biological_processglucan catabolic process
A0009277cellular_componentfungal-type cell wall
A0009986cellular_componentcell surface
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0031505biological_processfungal-type cell wall organization
A0044042biological_processglucan metabolic process
A0071555biological_processcell wall organization
B0000272biological_processpolysaccharide catabolic process
B0000324cellular_componentfungal-type vacuole
B0004338molecular_functionglucan exo-1,3-beta-glucosidase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0009251biological_processglucan catabolic process
B0009277cellular_componentfungal-type cell wall
B0009986cellular_componentcell surface
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0031505biological_processfungal-type cell wall organization
B0044042biological_processglucan metabolic process
B0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00659
Number of Residues10
DetailsGLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. IGIELINEPL
ChainResidueDetails
AILE225-LEU234

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AGLU232
BGLU232

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AGLU334
BGLU334

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14730348
ChainResidueDetails
AASN165
AASN325
BASN165
BASN325

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AGLU334
AASN231
ATYR297
AHIS295
AGLU232

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
BGLU334
BASN231
BTYR297
BHIS295
BGLU232

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AGLU334
AGLU232

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
BGLU334
BGLU232

site_idCSA5
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
AASN231
ATYR297
AGLU318
AHIS295
AGLU232

site_idCSA6
Number of Residues5
DetailsAnnotated By Reference To The Literature 1bqc
ChainResidueDetails
BASN231
BTYR297
BGLU318
BHIS295
BGLU232

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PDB entries from 2024-09-11

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