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6PMD

Structure of ClpP from Staphylococcus aureus in complex with Acyldepsipeptide

Summary for 6PMD
Entry DOI10.2210/pdb6pmd/pdb
Related5VZ2 5W18 6PKA
Related PRD IDPRD_002357
DescriptorATP-dependent Clp protease proteolytic subunit, SHV-WFP-SER-PRO-YCP-ALA-MP8 Acyldepsipeptide, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
Functional Keywordsclpp adep, antibiotic, hydrolase-antibiotic complex, hydrolase/antibiotic
Biological sourceStaphylococcus aureus (strain NCTC 8325)
More
Total number of polymer chains25
Total formula weight326861.87
Authors
Griffith, E.C.,Lee, R.E. (deposition date: 2019-07-01, release date: 2019-11-06, Last modification date: 2023-11-15)
Primary citationGriffith, E.C.,Zhao, Y.,Singh, A.P.,Conlon, B.P.,Tangallapally, R.,Shadrick, W.R.,Liu, J.,Wallace, M.J.,Yang, L.,Elmore, J.M.,Li, Y.,Zheng, Z.,Miller, D.J.,Cheramie, M.N.,Lee, R.B.,LaFleur, M.D.,Lewis, K.,Lee, R.E.
Ureadepsipeptides as ClpP Activators.
Acs Infect Dis., 5:1915-1925, 2019
Cited by
PubMed: 31588734
DOI: 10.1021/acsinfecdis.9b00245
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.21 Å)
Structure validation

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