X-ray diffraction
1.95Å resolution

A Second Divalent Metal Ion in the Active Site of a New Crystal Form of Human Apurinic/Apyridinimic Endonuclease, Ape1, and its Implications for the Catalytic Mechanism


Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
DNA-(apurinic or apyrimidinic site) endonuclease Chain: A
Molecule details ›
Chain: A
Length: 318 amino acids
Theoretical weight: 35.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P27695 (Residues: 1-318; Coverage: 100%)
Gene names: APE, APE1, APEX, APEX1, APX, HAP1, REF1
Structure domains: Endonuclease/exonuclease/phosphatase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL1-5
Spacegroup: C2
Unit cell:
a: 128.39Å b: 44.85Å c: 78.14Å
α: 90° β: 124.54° γ: 90°
R R work R free
0.205 0.205 0.255
Expression system: Escherichia coli BL21(DE3)