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-Structure paper
Title | Human cGAS catalytic domain has an additional DNA-binding interface that enhances enzymatic activity and liquid-phase condensation. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 116, Page 11946-11955, Year 2019 |
Publish date | Aug 9, 2018 (structure data deposition date) |
![]() | Xie, W. / Lama, L. / Adura, C. / Tomita, D. / Glickman, J.F. / Tuschl, T. / Patel, D.J. |
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Methods | X-ray diffraction |
Resolution | 2.196 - 3.209 Å |
Structure data | ![]() PDB-6edb: ![]() PDB-6edc: ![]() PDB-6o47: |
Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-CIT: ![]() ChemComp-LLS: ![]() ChemComp-AEV: ![]() ChemComp-HOH: |
Source |
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![]() | Transferase/DNA / SRY human cGAS DNA complex / Transferase-DNA complex / human cGAS DNA complex / TRANSFERASE / human / cGAS / core domain / compound / RU-521 / DNA BINDING PROTEIN |