5NIJ
Crystal structure of arabidopsis thaliana legumain isoform gamma in two-chain activation state
Summary for 5NIJ
Entry DOI | 10.2210/pdb5nij/pdb |
Descriptor | Vacuolar-processing enzyme gamma-isozyme, SULFATE ION, CITRIC ACID, ... (4 entities in total) |
Functional Keywords | asparaginyl endopeptidase, vacuolar processing enzyme, ligase, cysteine protease |
Biological source | Arabidopsis thaliana (Mouse-ear cress) |
Cellular location | Vacuole : Q39119 |
Total number of polymer chains | 4 |
Total formula weight | 202813.64 |
Authors | Zauner, F.B.,Dall, E.,Brandstetter, H. (deposition date: 2017-03-24, release date: 2018-02-28, Last modification date: 2024-01-17) |
Primary citation | Zauner, F.B.,Dall, E.,Regl, C.,Grassi, L.,Huber, C.G.,Cabrele, C.,Brandstetter, H. Crystal Structure of Plant Legumain Reveals a Unique Two-Chain State with pH-Dependent Activity Regulation. Plant Cell, 30:686-699, 2018 Cited by PubMed: 29453229DOI: 10.1105/tpc.17.00963 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.75 Å) |
Structure validation
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