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Structure paper

TitleHuman cGAS catalytic domain has an additional DNA-binding interface that enhances enzymatic activity and liquid-phase condensation.
Journal, issue, pagesProc. Natl. Acad. Sci. USA, Vol. 116, Page 11946-11955, Year 2019
Publish dateAug 9, 2018 (structure data deposition date)
AuthorsXie, W. / Lama, L. / Adura, C. / Tomita, D. / Glickman, J.F. / Tuschl, T. / Patel, D.J.
External linksProc. Natl. Acad. Sci. USA / PubMed:31142647
MethodsX-ray diffraction
Resolution2.196 - 3.209 Å
Structure data

PDB-6edb:
Crystal structure of SRY.hcGAS-21bp dsDNA complex
Method: X-RAY DIFFRACTION / Resolution: 3.209 Å

PDB-6edc:
hcGAS-16bp dsDNA complex
Method: X-RAY DIFFRACTION / Resolution: 2.712 Å

PDB-6o47:
human cGAS core domain (K427E/K428E) bound with RU-521
Method: X-RAY DIFFRACTION / Resolution: 2.196 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CIT:
CITRIC ACID

ChemComp-LLS:
(3~{S})-3-[1-[4,5-bis(chloranyl)-1~{H}-benzimidazol-2-yl]-3-methyl-5-oxidanyl-pyrazol-4-yl]-3~{H}-2-benzofuran-1-one

ChemComp-AEV:
2-(4,5-dichloro-1H-benzimidazol-2-yl)-5-methyl-4-[(1R)-3-oxo-1,3-dihydro-2-benzofuran-1-yl]-1,2-dihydro-3H-pyrazol-3-one

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsTransferase/DNA / SRY human cGAS DNA complex / Transferase-DNA complex / human cGAS DNA complex / TRANSFERASE / human / cGAS / core domain / compound / RU-521 / DNA BINDING PROTEIN

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