4D2X
Negative-stain electron microscopy of E. coli ClpB of Y503D hyperactive mutant (BAP form bound to ClpP)
Summary for 4D2X
| Entry DOI | 10.2210/pdb4d2x/pdb |
| Related | 4D2Q 4D2U |
| EMDB information | 2559 |
| Descriptor | CHAPERONE PROTEIN CLPB (1 entity in total) |
| Functional Keywords | chaperone, disaggregase, clpb, bap, y503d hyperactive mutant, coiled- coil domain |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 6 |
| Total formula weight | 581010.52 |
| Authors | Carroni, M.,Kummer, E.,Oguchi, Y.,Clare, D.K.,Wendler, P.,Sinning, I.,Kopp, J.,Mogk, A.,Bukau, B.,Saibil, H.R. (deposition date: 2014-05-13, release date: 2014-06-04, Last modification date: 2019-01-23) |
| Primary citation | Carroni, M.,Kummer, E.,Oguchi, Y.,Wendler, P.,Clare, D.K.,Sinning, I.,Kopp, J.,Mogk, A.,Bukau, B.,Saibil, H.R. Head-to-Tail Interactions of the Coiled-Coil Domains Regulate Clpb Activity and Cooperation with Hsp70 in Protein Disaggregation. Elife, 3:02481-, 2014 Cited by PubMed: 24843029DOI: 10.7554/ELIFE.02481 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (20 Å) |
Structure validation
Download full validation report
