6cwx

X-ray diffraction
2.25Å resolution

Crystal structure of human ribonuclease P/MRP proteins Rpp20/Rpp25

Released:

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Biochemical function:
Biological process:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero 48-mer
Assembly name:
PDBe Complex ID:
PDB-CPX-131129 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ribonuclease P protein subunit p20 Chain: A
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 16.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O75817 (Residues: 1-140; Coverage: 100%)
Gene names: POP7, RPP20
Sequence domains: Rpp20 subunit of nuclear RNase MRP and P
Ribonuclease P protein subunit p25 Chain: B
Molecule details ›
Chain: B
Length: 201 amino acids
Theoretical weight: 20.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BUL9 (Residues: 1-199; Coverage: 100%)
Gene name: RPP25
Sequence domains: Alba

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: I432
Unit cell:
a: 182.19Å b: 182.19Å c: 182.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.213 0.232
Expression system: Escherichia coli