1tg6

X-ray diffraction
2.1Å resolution

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP

Released:

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:
Cellular component:

Structure analysis Details

Assemblies composition:
homo heptamer (preferred)
homo tetradecamer
PDBe Complex ID:
PDB-CPX-172564 (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: 277 amino acids
Theoretical weight: 30.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q16740 (Residues: 1-277; Coverage: 100%)
Gene name: CLPP
Sequence domains: Clp protease
Structure domains: 2-enoyl-CoA Hydratase; Chain A, domain 1

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 162.57Å b: 119.002Å c: 118.65Å
α: 90° β: 130.159° γ: 90°
R-values:
R R work R free
0.28 0.224 0.262
Expression system: Escherichia coli BL21