3RWK
First crystal structure of an endo-inulinase, from Aspergillus ficuum: structural analysis and comparison with other GH32 enzymes.
Summary for 3RWK
Entry DOI | 10.2210/pdb3rwk/pdb |
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, ... (8 entities in total) |
Functional Keywords | endo-inulinase, glycoside hydrolase family 32, catalytic mechanism, glycosidase hydrolase family 32, glycosylation, cytosol, hydrolase |
Biological source | Aspergillus ficuum |
Cellular location | Secreted: O94220 |
Total number of polymer chains | 1 |
Total formula weight | 57460.96 |
Authors | Michaux, C.,Pouyez, J.,Roussel, G.,Mayard, A.,Vandamme, A.M.,Housen, I.,Wouters, J. (deposition date: 2011-05-09, release date: 2012-07-18, 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 (2.1 Å) |
Structure validation
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