3SC7
First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.
Summary for 3SC7
Entry DOI | 10.2210/pdb3sc7/pdb |
Related | 3RWK |
Descriptor | Inulinase, alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total) |
Functional Keywords | glycoside hydrolase family 32, endo-inulinase, glycosylation, cytosol, hydrolase |
Biological source | Aspergillus ficuum |
Cellular location | Secreted: O94220 |
Total number of polymer chains | 1 |
Total formula weight | 57160.85 |
Authors | Housen, I.,Pouyez, J.,Roussel, G.,Mayard, A.,Vandamme, A.M.,Wouters, J.,Michaux, C. (deposition date: 2011-06-07, release date: 2012-06-27, Last modification date: 2020-07-29) |
Primary citation | Pouyez, J.,Mayard, A.,Vandamme, A.M.,Roussel, G.,Perpete, E.A.,Wouters, J.,Housen, I.,Michaux, C. First crystal structure of an endo-inulinase, INU2, from Aspergillus ficuum: Discovery of an extra-pocket in the catalytic domain responsible for its endo-activity. Biochimie, 94:2423-2430, 2012 Cited by PubMed: 22750808DOI: 10.1016/j.biochi.2012.06.020 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
Download full validation report