3LJC
Crystal structure of Lon N-terminal domain.
Summary for 3LJC
Entry DOI | 10.2210/pdb3ljc/pdb |
Related | 2ANE |
Descriptor | ATP-dependent protease La (1 entity in total) |
Functional Keywords | lon n-domain, allosteric enzyme, atp-binding, dna-binding, hydrolase, nucleotide-binding, protease, serine protease, stress response |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A9M0 |
Total number of polymer chains | 1 |
Total formula weight | 29574.96 |
Authors | Li, M.,Gustchina, A.,Dauter, Z.,Wlodawer, A. (deposition date: 2010-01-26, release date: 2010-07-21, Last modification date: 2017-11-01) |
Primary citation | Li, M.,Gustchina, A.,Rasulova, F.S.,Melnikov, E.E.,Maurizi, M.R.,Rotanova, T.V.,Dauter, Z.,Wlodawer, A. Structure of the N-terminal fragment of Escherichia coli Lon protease Acta Crystallogr.,Sect.D, 66:865-873, 2010 Cited by PubMed: 20693685DOI: 10.1107/S0907444910019554 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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