1H4P
Crystal structure of exo-1,3-beta glucanse from Saccharomyces cerevisiae
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0000324 | cellular_component | fungal-type vacuole |
A | 0004338 | molecular_function | glucan exo-1,3-beta-glucosidase activity |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0005576 | cellular_component | extracellular region |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0009251 | biological_process | glucan catabolic process |
A | 0009277 | cellular_component | fungal-type cell wall |
A | 0009986 | cellular_component | cell surface |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0031505 | biological_process | fungal-type cell wall organization |
A | 0044042 | biological_process | glucan metabolic process |
A | 0071555 | biological_process | cell wall organization |
B | 0000272 | biological_process | polysaccharide catabolic process |
B | 0000324 | cellular_component | fungal-type vacuole |
B | 0004338 | molecular_function | glucan exo-1,3-beta-glucosidase activity |
B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
B | 0005576 | cellular_component | extracellular region |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0009251 | biological_process | glucan catabolic process |
B | 0009277 | cellular_component | fungal-type cell wall |
B | 0009986 | cellular_component | cell surface |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0031505 | biological_process | fungal-type cell wall organization |
B | 0044042 | biological_process | glucan metabolic process |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PROSITE/UniProt
site_id | PS00659 |
Number of Residues | 10 |
Details | GLYCOSYL_HYDROL_F5 Glycosyl hydrolases family 5 signature. IGIELINEPL |
Chain | Residue | Details |
A | ILE225-LEU234 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | GLU232 | |
B | GLU232 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000250 |
Chain | Residue | Details |
A | GLU334 | |
B | GLU334 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14730348 |
Chain | Residue | Details |
A | ASN165 | |
A | ASN325 | |
B | ASN165 | |
B | ASN325 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1bqc |
Chain | Residue | Details |
A | GLU334 | |
A | ASN231 | |
A | TYR297 | |
A | HIS295 | |
A | GLU232 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1bqc |
Chain | Residue | Details |
B | GLU334 | |
B | ASN231 | |
B | TYR297 | |
B | HIS295 | |
B | GLU232 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bqc |
Chain | Residue | Details |
A | GLU334 | |
A | GLU232 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bqc |
Chain | Residue | Details |
B | GLU334 | |
B | GLU232 |
site_id | CSA5 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1bqc |
Chain | Residue | Details |
A | ASN231 | |
A | TYR297 | |
A | GLU318 | |
A | HIS295 | |
A | GLU232 |
site_id | CSA6 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1bqc |
Chain | Residue | Details |
B | ASN231 | |
B | TYR297 | |
B | GLU318 | |
B | HIS295 | |
B | GLU232 |