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1Y9M

Crystal structure of exo-inulinase from Aspergillus awamori in spacegroup P212121

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004575molecular_functionsucrose alpha-glucosidase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0005987biological_processsucrose catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0051669molecular_functionfructan beta-fructosidase activity
A0051670molecular_functioninulinase activity
Functional Information from PROSITE/UniProt
site_idPS00609
Number of Residues14
DetailsGLYCOSYL_HYDROL_F32 Glycosyl hydrolases family 32 active site. HfsPqknwMNDPNG
ChainResidueDetails
AHIS31-GLY44

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10067","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10067","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15522299","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y9G","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"39357631","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15522299","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39357631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y4W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y9G","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"39357631","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15522299","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y9M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15522299","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"39357631","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1Y4W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y9G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1Y9M","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 15522299
ChainResidueDetails
AGLU241
AASP41

site_idMCSA1
Number of Residues2
DetailsM-CSA 827
ChainResidueDetails
AASP41covalently attached, nucleofuge, nucleophile
AGLU241activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor

246031

PDB entries from 2025-12-10

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