X-ray diffraction
2.4Å resolution

Structure of ClpP from Bacillus subtilis in monoclinic crystal form


Function and Biology Details

Reaction catalysed:
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-Casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec; and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).

Structure analysis Details

Assembly composition:
homo heptamer (preferred)
Entry contents:
1 distinct polypeptide molecule
ATP-dependent Clp protease proteolytic subunit Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 199 amino acids
Theoretical weight: 22.04 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P80244 (Residues: 2-197; Coverage: 100%)
Gene names: BSU34540, clpP, yvdN
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: C2
Unit cell:
a: 121.5Å b: 150.701Å c: 106.543Å
α: 90° β: 121.65° γ: 90°
R R work R free
0.212 0.212 0.268
Expression system: Escherichia coli BL21(DE3)