6ahv

X-ray diffraction
2.6Å resolution

Crystal structure of human RPP40

Released:
Source organism: Homo sapiens
Primary publication:
Cryo-EM Structure of the Human Ribonuclease P Holoenzyme.
Cell 175 1393-1404.e11 (2018)
PMID: 30454648

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:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease P protein subunit p40 Chain: A
Molecule details ›
Chain: A
Length: 363 amino acids
Theoretical weight: 41.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75818 (Residues: 1-363; Coverage: 100%)
Gene names: RNASEP1, RPP40
Sequence domains: Ribonuclease P 40kDa (Rpp40) subunit

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL18U1
Spacegroup: C2221
Unit cell:
a: 73.398Å b: 129.892Å c: 116.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.218 0.253
Expression system: Escherichia coli BL21(DE3)