1oqk

Solution NMR

Structure of Mth11: A homologue of human RNase P protein Rpp29

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-127818 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease P protein component 1 Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 11.16 KDa
Source organism: Methanothermobacter thermautotrophicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O26119 (Residues: 2-93; Coverage: 99%)
Gene names: MTH_11, rnp1
Sequence domains: Ribonuclease P/MRP, subunit p29
Structure domains: Ribonuclease P/MRP, subunit p29

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli