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; PubMed: 30790358; DOI: 10.1111/tpj.14293

Experimental method

X-RAY DIFFRACTION (3.1 Å)