› 7tqn

X-ray diffraction
1.8Å resolution

Structure of human TREX1

Released:
DOI: 10.2210/pdb7tqn/pdb
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PDB entry 7tqn coloured by chain, front view.
PDB entry 7tqn coloured by chain, side view.
PDB entry 7tqn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of human TREX1 DNA degradation and autoimmune disease.
Zhou W, Richmond-Buccola D, Wang Q, Kranzusch PJ
OpenAccess logo Nat Commun 13 4277 (2022)
PMID: 35879334

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
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192595 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Three-prime repair exonuclease 1 Chain: A
Molecule details ›
Chain: A
Length: 243 amino acids
Theoretical weight: 26.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NSU2 (Residues: 1-242; Coverage: 77%)
  • Best match: Q9NSU2-2 (Residues: 1-232)
Gene name: TREX1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 21-ID-E
Spacegroup: P41212
Unit cell:
a: 57.081Å b: 57.081Å c: 123.117Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.175 0.208
Expression system: Escherichia coli

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Citations

1 review citation

Molecular Mechanisms of Neutrophil Extracellular Trap (NETs) Degradation.
Demkow U. (2023)
7 other articles

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