2CE3

CRYSTAL STRUCTURE OF THE ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (CLPP1) FROM MYCOBACTERIUM TUBERCULOSIS

Summary for 2CE3

• Entry DOI: 10.2210/pdb2ce3/pdb
• Related: 2C8T 2CBY
• Descriptor: ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (2 entities in total)
• Functional Keywords: serine protease, clp protease, proteolytic subunit, endopeptidase, mycobacterium tuberculosis, atp-dependent protease, hydrolase
• Biological source: MYCOBACTERIUM TUBERCULOSIS (KOCH'S BACILLUS)
• Total number of polymer chains: 14
• Total formula weight: 304187.30

Authors

Segelke, B.,Kim, C.Y.,Ortiz-Lombardia, M.,Alzari, P.M.,Lekin, T. (deposition date: 2006-02-03, release date: 2006-02-09, Last modification date: 2023-12-13)

• Primary citation: Ingvarsson, H.,Mate, M.J.,Hogbom, M.,Portnoi, D.,Benaroudj, N.,Alzari, P.M.,Ortiz-Lombardia, M.,Unge, T.; Insights Into the Inter-Ring Plasticity of Caseinolytic Proteases from the X-Ray Structure of Mycobacterium Tuberculosis Clpp1.; Acta Crystallogr.,Sect.D, 63:249-, 2007; PubMed: 17242518; DOI: 10.1107/S0907444906050530

Experimental method

X-RAY DIFFRACTION (2.6 Å)