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Structure paper

TitleStructural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions.
Journal, issue, pagesJ. Biol. Chem., Vol. 296, Page 100692-100692, Year 2021
Publish dateJan 4, 2021 (structure data deposition date)
AuthorsPourfarjam, Y. / Ma, Z. / Kurinov, I. / Moss, J. / Kim, I.K.
External linksJ. Biol. Chem. / PubMed:33894202
MethodsX-ray diffraction
Resolution1.75 - 1.85 Å
Structure data

PDB-7l9f:
Crystal structure of human ARH3 bound to calcium and ADP-ribose
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-7l9h:
Crystal structure of human ARH3-D77A bound to magnesium and ADP-ribose
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

PDB-7l9i:
Crystal structure of human ARH3-D314A bound to magnesium and ADP-ribose
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-AR6:
[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsHYDROLASE / ADP-ribose / calcium / magnesium

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