wwPDB validation report of PDB entry 2CE3

ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1

THE 3.0 A RESOLUTION STRUCTURE OF CASEINOLYTIC CLP PROTEASE 1 FROM MYCOBACTERIUM TUBERCULOSIS

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

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT 1 (E.C.3.4.21.92)

CLPP ENDOPEPTIDASES ARE KNOWN TO BE
TETRADECAMERICAND THIS IS THE MULTIMERIC STATE FOUND
IN THISSTRUCTURE.HOWEVER, IN THIS PROTEIN, GEL
FILTRATION AND INTER-COMPLEX REGIONS BETWEEN THE
TWO HEPTAMERIC RINGS WOULDINDICATE THAT THE OLIGOMER
IS LIKELY TO BE HEPTAMERICIN SOLUTION.

The largest off-origin peak in the Patterson function is 3.44% of the height of the origin peak. No significant pseudotranslation is detected.

structure factor analysis and validation
geometric validation package for ligand chemistry in protein x-ray structures
20191225.v01 (using entries in the PDB archive December 25th 2019)