1y7o

X-ray diffraction
2.51Å resolution

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

Assemblies composition:
homo tetradecamer
homo heptamer (preferred)
PDBe Complex ID:
PDB-CPX-159120 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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: 218 amino acids
Theoretical weight: 24.28 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P63788 (Residues: 1-196; Coverage: 100%)
Gene names: clpP, spr0656
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P3221
Unit cell:
a: 105.65Å b: 105.65Å c: 236.192Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.192 0.186 0.248
Expression system: Escherichia coli