X-ray diffraction
2Å resolution

Structure of ClpP in complex with ADEP1


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:
hetero tetradecamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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: 21.99 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
  • 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
Acyldepsipeptide 1 Chains: H, I, J, K, L, M, N
Molecule details ›
Chains: H, I, J, K, L, M, N
Length: 7 amino acids
Theoretical weight: 737 Da
Source organism: Streptococcus hawaiiensis

Ligands and Environments

2 bound ligands:

2 modified residues:

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 121.645Å b: 151.756Å c: 100.665Å
α: 90° β: 120.03° γ: 90°
R R work R free
0.217 0.217 0.253
Expression system: Escherichia coli