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-Structure paper
| Title | Mutation of external glutamate residue reveals a new intermediate transport state and anion binding site in a CLC Cl-/H+antiporter. |
|---|---|
| Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 116, Page 17345-17354, Year 2019 |
| Publish date | Jul 31, 2018 (structure data deposition date) |
Authors | Park, K. / Lee, B.C. / Lim, H.H. |
External links | Proc. Natl. Acad. Sci. USA / PubMed:31409705 |
| Methods | X-ray diffraction |
| Resolution | 2.692 - 3.3 Å |
| Structure data | ![]() PDB-6ad7: ![]() PDB-6ad8: ![]() PDB-6ada: ![]() PDB-6adb: ![]() PDB-6adc: ![]() PDB-6k5a: ![]() PDB-6k5d: ![]() PDB-6k5f: ![]() PDB-6k5i: |
| Chemicals | ![]() ChemComp-BR: ![]() ChemComp-BXA: |
| Source |
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Keywords | TRANSPORT PROTEIN / CLC Cl-/H+ antiporter / intermediate structure / external glutamate / MEMBRANE PROTEIN / Cl- / H+ antiporter / CLC transporter / Cl-/H+ antiporter |
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