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Structure paper

TitleAPE1 active site residue Asn174 stabilizes the AP site and is essential for catalysis.
Journal, issue, pagesJ. Biol. Chem., Vol. 301, Page 110655-110655, Year 2025
Publish dateSep 20, 2024 (structure data deposition date)
AuthorsDeHart, K.M. / Hoitsma, N.M. / Thompson, S.H. / Borin, V.A. / Agarwal, P.K. / Freudenthal, B.D.
External linksJ. Biol. Chem. / PubMed:40902980
MethodsX-ray diffraction
Resolution1.99 - 2.29 Å
Structure data

PDB-9dp1:
APE1 N174A Substrate Complex with Abasic DNA
Method: X-RAY DIFFRACTION / Resolution: 2.29 Å

PDB-9dp2:
APE1 N174A Product Complex with Abasic DNA
Method: X-RAY DIFFRACTION / Resolution: 1.99 Å

PDB-9dp3:
APE1 N174D Product Complex with Abasic DNA
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-9dp4:
APE1 N174Q Product Complex with Abasic DNA
Method: X-RAY DIFFRACTION / Resolution: 2.25 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-MN:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-SO4:
SULFATE ION

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsHYDROLASE/DNA / APE1 / APEX1 / Endonuclease / DNA Repair / HYDROLASE-DNA complex

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