1Y9G
Crystal structure of exo-inulinase from Aspergillus awamori complexed with fructose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000272 | biological_process | polysaccharide catabolic process |
A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
A | 0004575 | molecular_function | sucrose alpha-glucosidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005737 | cellular_component | cytoplasm |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0005987 | biological_process | sucrose catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0051669 | molecular_function | fructan beta-fructosidase activity |
A | 0051670 | molecular_function | inulinase activity |
Functional Information from PROSITE/UniProt
site_id | PS00609 |
Number of Residues | 14 |
Details | GLYCOSYL_HYDROL_F32 Glycosyl hydrolases family 32 active site. HfsPqknwMNDPNG |
Chain | Residue | Details |
A | HIS31-GLY44 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU10067 |
Chain | Residue | Details |
A | ASP41 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|PROSITE-ProRule:PRU10067 |
Chain | Residue | Details |
A | GLU241 |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15522299, ECO:0007744|PDB:1Y9G |
Chain | Residue | Details |
A | ASN40 | |
A | ASP41 | |
A | GLN57 | |
A | TRP65 | |
A | SER103 | |
A | ARG188 | |
A | ASP189 | |
A | GLU241 | |
A | TRP335 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN49 | |
A | ASN112 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:39357631 |
Chain | Residue | Details |
A | ASN67 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15522299, ECO:0000269|PubMed:39357631, ECO:0007744|PDB:1Y4W, ECO:0007744|PDB:1Y9G |
Chain | Residue | Details |
A | ASN111 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255, ECO:0000269|PubMed:39357631 |
Chain | Residue | Details |
A | ASN254 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15522299, ECO:0007744|PDB:1Y9M |
Chain | Residue | Details |
A | ASN300 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15522299, ECO:0000269|PubMed:39357631, ECO:0007744|PDB:1Y4W, ECO:0007744|PDB:1Y9G, ECO:0007744|PDB:1Y9M |
Chain | Residue | Details |
A | ASN398 | |
A | ASN430 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1y9m |
Chain | Residue | Details |
A | GLU241 | |
A | ASP41 |
site_id | MCSA1 |
Number of Residues | 2 |
Details | M-CSA 827 |
Chain | Residue | Details |
A | ASP41 | covalently attached, nucleofuge, nucleophile |
A | GLU241 | activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |