1nz0

X-ray diffraction
1.2Å resolution

RNASE P PROTEIN FROM THERMOTOGA MARITIMA

Released:
Source organism: Thermotoga maritima

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
homo trimer
homo tetramer
PDBe Complex ID:
PDB-CPX-194798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease P protein component Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 118 amino acids
Theoretical weight: 14.43 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1H4 (Residues: 1-117; Coverage: 100%)
Gene names: TM_1463, rnpA
Sequence domains: Ribonuclease P
Structure domains: Ribosomal Protein S5; domain 2

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 56.227Å b: 64.143Å c: 68.326Å
α: 90° β: 102.02° γ: 90°
R-values:
R R work R free
0.163 0.162 0.217
Expression system: Escherichia coli