7uvr

X-ray diffraction
2.86Å resolution

Crystal structure of human ClpP protease in complex with TR-65

Released:
Model geometry
Fit model/data

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:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetradecamer (preferred)
PDBe Complex ID:
PDB-CPX-172563 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent Clp protease proteolytic subunit, mitochondrial Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 221 amino acids
Theoretical weight: 24.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16740 (Residues: 58-277; Coverage: 79%)
Gene name: CLPP
Sequence domains: Clp protease

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: C2
Unit cell:
a: 142.171Å b: 152.515Å c: 104.268Å
α: 90° β: 118.1° γ: 90°
R-values:
R R work R free
0.205 0.203 0.253
Expression system: Escherichia coli