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).
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
homo tetradecamer (preferred)
Assembly name:
Endopeptidase ClpP complex (preferred)
PDBe Complex ID:
PDB-CPX-141326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease proteolytic subunit
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N
Length: 193 amino acids
Theoretical weight: 21.59 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1
Length: 193 amino acids
Theoretical weight: 21.59 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
- Canonical:
P0A6G7 (Residues: 15-207; Coverage: 93%)
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
X-ray source:
NSLS BEAMLINE X12C
Spacegroup:
C2
Expression system: Not provided
