1RR9

Catalytic domain of E.coli Lon protease

Summary for 1RR9

• Entry DOI: 10.2210/pdb1rr9/pdb
• Related: 1RRE
• Descriptor: ATP-dependent protease La, SULFATE ION (3 entities in total)
• Functional Keywords: atp-dependent protease, catalytic dyad ser-lys, hydrolase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P0A9M0
• Total number of polymer chains: 6
• Total formula weight: 128679.32

Authors

Botos, I.,Melnikov, E.E.,Cherry, S.,Tropea, J.E.,Khalatova, A.G.,Dauter, Z.,Maurizi, M.R.,Rotanova, T.V.,Wlodawer, A.,Gustchina, A. (deposition date: 2003-12-08, release date: 2003-12-23, 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; PubMed: 14665623; DOI: 10.1074/jbc.M312243200

Experimental method

X-RAY DIFFRACTION (2.1 Å)