CLC-ec1 L25C/A450C/C85A at pH 4.5 100mM Cl Twist. Determined by electron microscopy at 2.9 Å resolution. Released 7 Feb 2024.
Explore 8GAH in 3D Show helices and sheets RCSB PDB PDBe
8GAH contains 50 α-helices and 10 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 34-45 | 12 | |
| α-helix | 51-65 | 15 | |
| α-helix | 75-100 | 26 | |
| β-strand | 106 | 1 | 1 |
| α-helix | 109-113 | 5 | |
| α-helix | 124-140 | 17 | |
| β-strand | 146 | 1 | 2 |
| α-helix | 148-165 | 18 | |
| α-helix | 171-174 | 4 | |
| α-helix | 176-189 | 14 | |
| α-helix | 193-202 | 10 | |
| β-strand | 209-211 | 3 | 3 |
| α-helix | 212-232 | 21 | |
| α-helix | 253-277 | 25 | |
| α-helix | 280-282 | 3 | |
| α-helix | 288-304 | 17 | |
| α-helix | 310-312 | 3 | |
| α-helix | 320-324 | 5 | |
| α-helix | 331-348 | 18 | |
| β-strand | 353 | 1 | 1 |
| β-strand | 355 | 1 | 2 |
| α-helix | 357-378 | 22 | |
| α-helix | 380-382 | 3 | |
| α-helix | 386-392 | 7 | |
| α-helix | 397-400 | 4 | |
| α-helix | 405-415 | 11 | |
| α-helix | 423-439 | 17 | |
| α-helix | 444-456 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 32-64 | 33 | |
| α-helix | 69-71 | 3 | |
| α-helix | 75-78 | 4 | |
| α-helix | 80-99 | 20 | |
| α-helix | 102-104 | 3 | |
| β-strand | 106 | 1 | 4 |
| α-helix | 109-112 | 4 | |
| α-helix | 127-130 | 4 | |
| α-helix | 133-138 | 6 | |
| β-strand | 146 | 1 | 5 |
| α-helix | 149-164 | 16 | |
| α-helix | 172-187 | 16 | |
| α-helix | 193-202 | 10 | |
| β-strand | 209-211 | 3 | 3 |
| α-helix | 212-232 | 21 | |
| α-helix | 244-248 | 5 | |
| α-helix | 249-251 | 3 | |
| α-helix | 254-280 | 27 | |
| α-helix | 288-304 | 17 | |
| α-helix | 320-324 | 5 | |
| α-helix | 330-348 | 19 | |
| β-strand | 353 | 1 | 4 |
| β-strand | 355 | 1 | 5 |
| α-helix | 357-374 | 18 | |
| α-helix | 386-392 | 7 | |
| α-helix | 393-396 | 4 | |
| α-helix | 398-402 | 5 | |
| α-helix | 405-412 | 8 | |
| α-helix | 419-421 | 3 | |
| α-helix | 422-427 | 6 | |
| α-helix | 434-439 | 6 | |
| α-helix | 444-459 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| H(+)/Cl(-) exchange transporter ClcA | A, B | protein | 461 | Escherichia coli | P37019 (AlphaFold model) |
>8GAH_1 H(+)/Cl(-) exchange transporter ClcA (chains A, B) MKTDTPSLETPQAARLRRRQLIRQCLERDKTPLAILFMAAVVGTLVGLAAVAFDKGVAWL QNQRMGALVHTADNYPLLLTVAFLASAVLAMFGYFLVRKYAPEAGGSGIPEIEGALEDQR PVRWWRVLPVKFFGGLGTLGGGMVLGREGPTVQIGGNIGRMVLDIFRLKGDEARHTLLAT GAAAGLAAAFNAPLAGILFIIEEMRPQFRYTLISIKAVFIGVIMSTIMYRIFNHEVALID VGKLSDAPLNTLWLYLILGIIFGIFGPIFNKWVLGMQDLLHRVHGGNITKWVLMGGAIGG LCGLLGFVAPATSGGGFNLIPIATAGNFSMGMLVFIFVARVITTLLCFSSGAPGGIFAPM LALGTVLGTAFGMVAVELFPQYHLEAGTFAIAGMGALLAASIRAPLTGIILVLEMTDNYQ LILPMIITGLGATLLAQFTGGKPLYSAILCRTLAKQEAEQL
Structural basis of pH-dependent activation in a CLC transporter. Fortea, E., Lee, S., Chadda, R. et al. Nat Struct Mol Biol (2024) 31:644-656. DOI 10.1038/s41594-023-01210-5 · PubMed
Other PDB entries of the same protein (UniProt P37019 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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