ClpP     DOI:10.2210/pdb1yg6/pdb

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Primary Citation       Molecular Description Hide Classification: Hydrolase Structure Weight: 303872.45   Molecule: ATP-dependent Clp protease proteolytic subunit Polymer: 1 Type: polypeptide(L) Length: 193 Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N EC#: 3.4.21.92          Source Hide Polymer: 1 Scientific Name: Escherichia coli Expression System: Escherichia coli         Related PDB Entries Hide Id Details 1TYF  The Structure Of Clpp At 2.3 Angstrom Resolution Suggests A Model For ATP-Dependent Proteolysis        Ligand Chemical Component Hide Identifier Name Formula Interaction View Links MPD     (4S)-2-METHYL-2,4-PENTANEDIOL C6 H14 O2 Ligand Explorer       Derived Data Hide SCOP Classification v1.75 - (14 Domains) CATH Classification v3.2.0 - (14 Domains) PFAM Classification - (14 Domains) GO Terms - (13 Terms)     Reset Layout

Biological Assembly     More Images... View in Jmol Other Viewers close KiNG WebMol QuickPDB FirstGlance Kiosk SimpleViewer Protein Workshop Ligand Explorer Biological assembly assigned by authors and generated by PISA (software)         Deposition Summary Hide Authors:   Bewley, M.C.,   Graziano, V.,   Griffin, K.,   Flanagan, J.M. Deposition:   2005-01-04 Release:   2006-04-04 Last Modified (REVDAT):   2009-02-24       Experimental Details Hide Method:   X-RAY DIFFRACTION Experimental Data:   N/A Resolution[Å]: 1.90 R-Value: 0.228 (obs.) R-Free: 0.251 Space Group: C 2 Unit Cell:   Length [Å] Angles [°] a = 192.50 α = 90.00  b = 103.30 β = 98.40  c = 159.00 γ = 90.00