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-Structure paper
Title | Structure of the N-terminal domain of ClpC1 in complex with the antituberculosis natural product ecumicin reveals unique binding interactions. |
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Journal, issue, pages | Acta Crystallogr D Struct Biol, Vol. 76, Page 458-471, Year 2020 |
Publish date | Jun 13, 2019 (structure data deposition date) |
Authors | Wolf, N.M. / Lee, H. / Zagal, D. / Nam, J.W. / Oh, D.C. / Suh, J.W. / Pauli, G.F. / Cho, S. / Abad-Zapatero, C. |
External links | Acta Crystallogr D Struct Biol / PubMed:32355042 |
Methods | X-ray diffraction |
Resolution | 1.6 - 2.5 Å |
Structure data | PDB-6pba: PDB-6pbq: PDB-6pbs: PDB-6ucr: |
Chemicals | ChemComp-HOH: ChemComp-PO4: ChemComp-EPE: ChemComp-ACT: |
Source |
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Keywords | CHAPERONE / ClpC1-NTD / ATPase / Clp protease / Ecumicin / Mycobacterium tuberculosis / CHAPERONE/ANTIBIOTIC / CHAPERONE-ANTIBIOTIC complex |