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: 31925204 DOI: 10.1038/s42003-019-0656-3 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation