Function and Biology Details
Reaction catalysed:
Release of N-terminal targeting peptides from precursor proteins imported into the mitochondrion, typically with Arg in position P2.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Mitochondrial processing peptidase complex (preferred)
PDBe Complex ID:
PDB-CPX-145324 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mitochondrial-processing peptidase subunit alpha
Molecule details ›
Chains: A, C, E, G
Length: 475 amino acids
Theoretical weight: 52.53 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
Length: 475 amino acids
Theoretical weight: 52.53 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P11914 (Residues: 14-482; Coverage: 97%)
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
Mitochondrial-processing peptidase subunit beta
Molecule details ›
Chains: B, D, F, H
Length: 443 amino acids
Theoretical weight: 48.9 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
Length: 443 amino acids
Theoretical weight: 48.9 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P10507 (Residues: 21-462; Coverage: 96%)
Sequence domains:
Structure domains: Metalloenzyme, LuxS/M16 peptidase-like
