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-Structure paper
Title | The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site |
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Journal, issue, pages | J. Biol. Chem., Vol. 279, Page 8140-8148, Year 2004 |
Publish date | Dec 8, 2003 (structure data deposition date) |
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. |
External links | J. Biol. Chem. / PubMed:14665623 |
Methods | X-ray diffraction |
Resolution | 1.75 - 2.1 Å |
Structure data | PDB-1rr9: PDB-1rre: |
Chemicals | ChemComp-SO4: ChemComp-HOH: |
Source |
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Keywords | HYDROLASE / ATP-dependent protease / catalytic dyad Ser-Lys / catalytic Ser-Lys dyad |