4rou

X-ray diffraction
2.71Å resolution

Auto-inhibition Mechanism of Human Mitochondrial RNase P Protein Complex

Released:
Source organism: Homo sapiens
Entry authors: Li F, Liu X, Yang X, Shen Y

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Biochemical function:
  • not assigned
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-127287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitochondrial ribonuclease P catalytic subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 310 amino acids
Theoretical weight: 36.12 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: O15091 (Residues: 274-583; Coverage: 53%)
Gene names: KIAA0391, MRPP3, PRORP
Sequence domains: Protein-only RNase P

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P212121
Unit cell:
a: 66.434Å b: 78.287Å c: 114.187Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.24 0.238 0.278