1RRE
Crystal structure of E.coli Lon proteolytic domain
Summary for 1RRE
Entry DOI | 10.2210/pdb1rre/pdb |
Related | 1RR9 |
Descriptor | ATP-dependent protease La, SULFATE ION (3 entities in total) |
Functional Keywords | atp-dependent protease, catalytic ser-lys dyad, hydrolase |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A9M0 |
Total number of polymer chains | 6 |
Total formula weight | 129804.80 |
Authors | Botos, I.,Melnikov, E.E.,Cherry, S.,Tropea, J.E.,Khalatova, A.G.,Rasulova, F.,Dauter, Z.,Maurizi, M.R.,Rotanova, T.V.,Wlodawer, A.,Gustchina, A. (deposition date: 2003-12-08, release date: 2004-02-03, Last modification date: 2021-10-27) |
Primary citation | Botos, I.,Melnikov, E.E.,Cherry, S.,Tropea, J.E.,Khalatova, A.G.,Rasulova, F.,Dauter, Z.,Maurizi, M.R.,Rotanova, T.V.,Wlodawer, A.,Gustchina, A. The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site J.Biol.Chem., 279:8140-8148, 2004 Cited by PubMed: 14665623DOI: 10.1074/jbc.M312243200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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