› 8hcf

X-ray diffraction
1.6Å resolution

Crystal structure of mTREX1-UMP complex

Released:
DOI: 10.2210/pdb8hcf/pdb
PDB entry 8hcf coloured by chain, front view.
PDB entry 8hcf coloured by chain, side view.
PDB entry 8hcf coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Molecular insight into the specific enzymatic properties of TREX1 revealing the diverse functions in processing RNA and DNA/RNA hybrids.
Huang KW, Wu CY, Toh SI, Liu TC, Tu CI, Lin YH, Cheng AJ, Kao YT, Chu JW, Hsiao YY
OpenAccess logo Nucleic Acids Res (2023)
PMID: 37870446

Function and Biology Details

Reaction catalysed: 
Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187588 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Three-prime repair exonuclease 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 27.4 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q91XB0 (Residues: 1-242; Coverage: 77%)
Gene name: Trex1

Ligands and Environments

3 bound ligands:
Ligand EPE 1 x EPE
Ligand SO4 3 x SO4
Ligand U5P 1 x U5P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 64.031Å b: 85.771Å c: 100.035Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.179
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Molecular insight into the specific enzymatic properties of TREX1 revealing the diverse functions in processing RNA and DNA/RNA hybrids.
Huang et al. (2023)