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3SC7

First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.

Functional Information from GO Data
ChainGOidnamespacecontents
X0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
X0005975biological_processcarbohydrate metabolic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22750808","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
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":"22750808","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-12-17

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