› 3fes

X-ray diffraction
1.82Å resolution

Crystal Structure of the ATP-dependent Clp Protease ClpC from Clostridium difficile

Released:
DOI: 10.2210/pdb3fes/pdb
PDB entry 3fes coloured by chain, front view.
PDB entry 3fes coloured by chain, side view.
PDB entry 3fes coloured by chain, top view.
Source organism: Clostridioides difficile 630
Entry authors: Kim Y, Tesar C, Li H, Cobb G, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172739 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Class III stress response-related ATPase, AAA+ superfamily Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 145 amino acids
Theoretical weight: 16.05 KDa
Source organism: Clostridioides difficile 630
Expression system: Escherichia coli
UniProt:
  • Canonical: Q18CA9 (Residues: 2-143; Coverage: 17%)
Gene names: CD630_00260, clpC
Sequence domains: Clp amino terminal domain, pathogenicity island component
Structure domains: Clp, N-terminal domain

Ligands and Environments

3 bound ligands:
Ligand MG 4 x MG
Ligand PG4 4 x PG4
Ligand EPE 1 x EPE
1 modified residue:
Ligand MSE 16 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 34.69Å b: 68.523Å c: 81.339Å
α: 66.91° β: 86.23° γ: 85.33°
R-values:
R R work R free
0.189 0.187 0.222
Expression system: Escherichia coli

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