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Summary Structural Experimental Function Sequence Neighbor Download Link


<Asymmetric unit>

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PDB ID2c8t  sequence information (FASTA format)   
DescriptorATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (E.C.3.4.21.92)
TitleTHE 3.0 A RESOLUTION STRUCTURE OF CASEINOLYTIC CLP PROTEASE 1 FROM MYCOBACTERIUM TUBERCULOSIS
Functional KeywordsCASEINOLYTIC CLP PROTEASE 1, PROTEASE, SERINE PROTEASE, CLPP1, TETRADECAMER, HYDROLASE
Biological sourceMYCOBACTERIUM TUBERCULOSIS
Total number of polymer chains14
Total molecular weight313719 (the details in Structural Details Page)
AuthorsIngvarsson, H. , Hogbom, M. , Jones, T.A. , Unge, T. (deposition date : 2005-12-07, release date : 2007-02-06)
Primary citationIngvarsson, 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 methodX-RAY DIFFRACTION ( 3.00[Å] )
Other Database Information
Yorodumi , CATH , CE , FSSP , SCOP , VAST , UniProt ( P0A526 ) , eF-site , KEGG ( EC 3.4.21.92 ) , PISA