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2X36

Structure of the proteolytic domain of the Human Mitochondrial Lon protease

Summary for 2X36
Entry DOI10.2210/pdb2x36/pdb
DescriptorLON PROTEASE HOMOLOG, MITOCHONDRIAL (2 entities in total)
Functional Keywordshydrolase, catalytic dyad, transit peptide, mitochondria
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationMitochondrion matrix: P36776
Total number of polymer chains6
Total formula weight134554.30
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 citationGarcia-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: 20222013
DOI: 10.1002/PRO.376
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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