› 3hws

X-ray diffraction
3.25Å resolution

Crystal structure of nucleotide-bound hexameric ClpX

Released:
DOI: 10.2210/pdb3hws/pdb
PDB entry 3hws coloured by chain, front view.
PDB entry 3hws coloured by chain, side view.
PDB entry 3hws coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.
Glynn SE, Martin A, Nager AR, Baker TA, Sauer RT
Cell 139 744-56 (2009)
PMID: 19914167

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo hexamer
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141343 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease ATP-binding subunit ClpX Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 363 amino acids
Theoretical weight: 39.43 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6H1 (Residues: 62-424; Coverage: 86%)
Gene names: JW0428, b0438, clpX, lopC
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ADP 4 x ADP
Ligand SO4 13 x SO4
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 54.085Å b: 178.498Å c: 201.369Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.243 0.282
Expression system: Escherichia coli

Quick links

Citations

41 review citations

AAA+ proteases: ATP-fueled machines of protein destruction.
Sauer et al. (2011)
40 more

25 mentions without citation

Chaperone machines for protein folding, unfolding and disaggregation.
Saibil H. (2013)
24 more