2X36
Structure of the proteolytic domain of the Human Mitochondrial Lon protease
Summary for 2X36
Entry DOI | 10.2210/pdb2x36/pdb |
Descriptor | LON PROTEASE HOMOLOG, MITOCHONDRIAL (2 entities in total) |
Functional Keywords | hydrolase, catalytic dyad, transit peptide, mitochondria |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Mitochondrion matrix: P36776 |
Total number of polymer chains | 6 |
Total formula weight | 134554.30 |
Authors | Garcia, J.,Ondrovicova, G.,Blagova, E.,Levdikov, V.M.,Bauer, J.A.,Kutejova, E.,Wilkinson, A.J.,Wilson, K.S. (deposition date: 2010-01-21, release date: 2010-05-19, Last modification date: 2023-12-20) |
Primary citation | Garcia-Nafria, J.,Ondrovicova, G.,Blagova, E.,Levdikov, V.M.,Bauer, J.A.,Suzuki, C.K.,Kutejova, E.,Wilkinson, A.J.,Wilson, K.S. Structure of the Catalytic Domain of the Human Mitochondrial Lon Protease: Proposed Relation of Oligomer Formation and Activity. Protein Sci., 19:987-, 2010 Cited by PubMed: 20222013DOI: 10.1002/PRO.376 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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