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| Title | The crystal structures of four peptide deformylases bound to the antibiotic actinonin reveal two distinct types: a platform for the structure-based design of antibacterial agents. |
|---|---|
| Journal, issue, pages | J. Mol. Biol., Vol. 320, Page 951-962, Year 2002 |
| Publish date | May 14, 2002 (structure data deposition date) |
Authors | Guilloteau, J.P. / Mathieu, M. / Giglione, C. / Blanc, V. / Dupuy, A. / Chevrier, M. / Gil, P. / Famechon, A. / Meinnel, T. / Mikol, V. |
External links | J. Mol. Biol. / PubMed:12126617 |
| Methods | X-ray diffraction |
| Resolution | 1.87 - 2.6 Å |
| Structure data | ![]() PDB-1lqw: ![]() PDB-1lqy: ![]() PDB-1lru: ![]() PDB-1lry: |
| Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-HOH: ![]() ChemComp-NI: ![]() ChemComp-BB2: ![]() ChemComp-SO4: |
| Source |
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Keywords | HYDROLASE / PDF / PEPTIDE DEFORMYLASE / ACTINONIN / INHIBITION / POLYPEPTIDE DEFORMYLASE |
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geobacillus stearothermophilus (bacteria)
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