3zwf

X-ray diffraction
1.7Å resolution

Crystal structure of Human tRNase Z, short form (ELAC1).

Released:
Source organism: Homo sapiens
Entry authors: Allerston CK, Krojer T, Berridge G, Burgess-Brown N, Chaikuad A, Chalk R, Elkins JM, Gileadi C, Latwiel SVA, Savitsky P, Vollmar M, Arrowsmith CH, Weigelt J, Edwards A, Bountra C, von Delft F, Gileadi O

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-190656 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Zinc phosphodiesterase ELAC protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 368 amino acids
Theoretical weight: 40.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9H777 (Residues: 3-363; Coverage: 99%)
Gene names: D29, ELAC1
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 59.52Å b: 73.79Å c: 73.66Å
α: 90° β: 98.69° γ: 90°
R-values:
R R work R free
0.188 0.187 0.21
Expression system: Escherichia coli BL21(DE3)