6DHI
Butelase 1: Auto-Catalytic Cleavage as an Evolutionary Constraint for Macrocyclizing Endopeptidases
Summary for 6DHI
Entry DOI | 10.2210/pdb6dhi/pdb |
Descriptor | Asparaginyl endopeptidase (2 entities in total) |
Functional Keywords | plant protein, hydrolase, asparaginyl endopeptidase |
Biological source | Clitoria ternatea (Butterfly pea) |
Total number of polymer chains | 4 |
Total formula weight | 210804.26 |
Authors | Bond, C.S.,Haywood, J. (deposition date: 2018-05-20, release date: 2018-08-15, Last modification date: 2023-11-15) |
Primary citation | James, A.M.,Haywood, J.,Leroux, J.,Ignasiak, K.,Elliott, A.G.,Schmidberger, J.W.,Fisher, M.F.,Nonis, S.G.,Fenske, R.,Bond, C.S.,Mylne, J.S. The macrocyclizing protease butelase 1 remains autocatalytic and reveals the structural basis for ligase activity. Plant J., 98:988-999, 2019 Cited by PubMed: 30790358DOI: 10.1111/tpj.14293 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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