6VFS
ClpXP from Neisseria meningitidis - Conformation A
Summary for 6VFS
Entry DOI | 10.2210/pdb6vfs/pdb |
Related | 6VFX |
EMDB information | 21187 21194 |
Descriptor | ATP-dependent Clp protease ATP-binding subunit ClpX, Unidentified protein substrate, ATP-dependent Clp protease proteolytic subunit, ... (6 entities in total) |
Functional Keywords | complex, aaa+, protease, clpp, clpx, hydrolase |
Biological source | Neisseria meningitidis More |
Total number of polymer chains | 21 |
Total formula weight | 592650.26 |
Authors | Ripstein, Z.A.,Vahidi, S.,Houry, W.A.,Rubinstein, J.L.,Kay, L.E. (deposition date: 2020-01-06, release date: 2020-01-22, Last modification date: 2024-03-06) |
Primary citation | Ripstein, Z.A.,Vahidi, S.,Houry, W.A.,Rubinstein, J.L.,Kay, L.E. A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery. Elife, 9:-, 2020 Cited by PubMed: 31916936DOI: 10.7554/eLife.52158 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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