6CN8
High-resolution structure of ClpC1-NTD binding to Rufomycin-I
Summary for 6CN8
Entry DOI | 10.2210/pdb6cn8/pdb |
Related PRD ID | PRD_002306 |
Descriptor | ATP-dependent Clp protease ATP-binding subunit ClpC1, Rufomycin I, PHOSPHATE ION, ... (6 entities in total) |
Functional Keywords | mycobacterium tuberculosis, rufomycin i, macrocyclic peptide, clpc1-ntd, chaperone, atp-dependent protease, chaperone-antibiotic complex, atpase aaa+, natural product, chaperone/antibiotic |
Biological source | Mycobacterium tuberculosis More |
Total number of polymer chains | 2 |
Total formula weight | 18922.15 |
Authors | Abad-Zapatero, C.,Wolf, N.W. (deposition date: 2018-03-07, release date: 2019-06-05, Last modification date: 2023-11-15) |
Primary citation | Wolf, N.M.,Lee, H.,Choules, M.P.,Pauli, G.F.,Phansalkar, R.,Anderson, J.R.,Gao, W.,Ren, J.,Santarsiero, B.D.,Lee, H.,Cheng, J.,Jin, Y.Y.,Ho, N.A.,Duc, N.M.,Suh, J.W.,Abad-Zapatero, C.,Cho, S. High-Resolution Structure of ClpC1-Rufomycin and Ligand Binding Studies Provide a Framework to Design and Optimize Anti-Tuberculosis Leads. Acs Infect Dis., 5:829-840, 2019 Cited by PubMed: 30990022DOI: 10.1021/acsinfecdis.8b00276 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
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