› 2o3h

X-ray diffraction
1.9Å resolution

Crystal structure of the human C65A Ape

Released:
DOI: 10.2210/pdb2o3h/pdb
PDB entry 2o3h coloured by chain, front view.
PDB entry 2o3h coloured by chain, side view.
PDB entry 2o3h coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Evolution of the redox function in mammalian apurinic/apyrimidinic endonuclease.
Georgiadis MM, Luo M, Gaur RK, Delaplane S, Li X, Kelley MR
Mutat Res 643 54-63 (2008)
PMID: 18579163

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA repair nuclease/redox regulator APEX1, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 285 amino acids
Theoretical weight: 32.01 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P27695 (Residues: 40-318; Coverage: 88%)
Gene names: APE, APE1, APEX, APEX1, APX, HAP1, REF1
Sequence domains: Endonuclease/Exonuclease/phosphatase family
Structure domains: Endonuclease/exonuclease/phosphatase

Ligands and Environments

2 bound ligands:
Ligand SM 2 x SM
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21212
Unit cell:
a: 46.693Å b: 143.604Å c: 45.385Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.226
Expression system: Escherichia coli

Quick links

Citations

24 review citations

The many functions of APE1/Ref-1: not only a DNA repair enzyme.
Tell et al. (2009)
23 more

5 mentions without citation

Association of DNA Repair Gene APE1 Asp148Glu Polymorphism with Breast Cancer Risk.
AlMutairi et al. (2015)
4 more