4jg4

X-ray diffraction
2.3Å resolution

Ligand concentration regulates the pathways of coupled protein folding and binding

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-150592 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease P protein component Chain: A
Molecule details ›
Chain: A
Length: 119 amino acids
Theoretical weight: 14.14 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P25814 (Residues: 1-116; Coverage: 100%)
Gene names: BSU41050, rnpA
Sequence domains: Ribonuclease P
Structure domains: Ribosomal Protein S5; domain 2

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P64
Unit cell:
a: 83.152Å b: 83.152Å c: 32.236Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.216 0.213 0.249
Expression system: Escherichia coli