THE STRUCTURE OF CLPP AT 2.3 ANGSTROM RESOLUTION SUGGESTS A MODEL FOR ATP-DEPENDENT PROTEOLYSIS     DOI:10.2210/pdb1tyf/pdb

1TYF Display Files close FASTA Sequence PDB File PDB File (Header) mmCIF File mmCIF File (Header) PDBML/XML File PDBML/XML File (Header) Download Files close FASTA Sequence PDB File (Text) PDB File (gz) mmCIF File mmCIF File (gz) PDBML/XML File PDBML/XML File (gz) Structure Factor (Text) Structure Factor (gz) Biological Assembly (gz) (A+S) Print this Page Share this Page close Email Delicious Stumble Google More... Link this Page

Primary Citation       Molecular Description Hide Classification: Peptidase Structure Weight: 302218.00   Molecule: CLP PEPTIDASE 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         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:   Wang, J.,   Hartling, J.A.,   Flanagan, J.M. Deposition:   1997-10-13 Release:   1998-06-17 Last Modified (REVDAT):   2009-02-24       Experimental Details Hide Method:   X-RAY DIFFRACTION Experimental Data:    [ EDS ] Resolution[Å]: 2.30 R-Value: 0.219 (obs.) R-Free: 0.292 Space Group: C 2 Unit Cell:   Length [Å] Angles [°] a = 193.32 α = 90.00  b = 102.46 β = 97.80  c = 157.08 γ = 90.00