6NAH
Crystal structure of Neisseria meningitidis ClpP protease in complex with Acyldepsipeptide-14 (ADEP-14)
Summary for 6NAH
Entry DOI | 10.2210/pdb6nah/pdb |
Descriptor | ATP-dependent Clp protease proteolytic subunit, Acyldepsipeptide-14, OCTANOIC ACID (CAPRYLIC ACID), ... (4 entities in total) |
Functional Keywords | serine protease, antibiotic, anticancer, hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor |
Biological source | Neisseria meningitidis More |
Total number of polymer chains | 56 |
Total formula weight | 706936.02 |
Authors | Mabanglo, M.F.,Houry, W.A. (deposition date: 2018-12-05, release date: 2019-11-13, Last modification date: 2023-11-15) |
Primary citation | Mabanglo, M.F.,Leung, E.,Vahidi, S.,Seraphim, T.V.,Eger, B.T.,Bryson, S.,Bhandari, V.,Zhou, J.L.,Mao, Y.Q.,Rizzolo, K.,Barghash, M.M.,Goodreid, J.D.,Phanse, S.,Babu, M.,Barbosa, L.R.S.,Ramos, C.H.I.,Batey, R.A.,Kay, L.E.,Pai, E.F.,Houry, W.A. ClpP protease activation results from the reorganization of the electrostatic interaction networks at the entrance pores. Commun Biol, 2:410-410, 2019 Cited by PubMed: 31925204DOI: 10.1038/s42003-019-0656-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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