Structure of an acid-sensing ion channel solubilized by styrene maleic acid and in a desensitized state at low pH. Determined by electron microscopy at 2.82 Å resolution. Released 11 Mar 2020.
Explore 6VTK in 3D Show helices and sheets RCSB PDB PDBe
6VTK contains 84 α-helices and 63 β-strands across 3 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 | 19-25 | 7 | |
| α-helix | 31-34 | 4 | |
| α-helix | 42-69 | 28 | |
| β-strand | 74-81 | 8 | 1 |
| β-strand | 86-87 | 2 | 2 |
| α-helix | 88 | 1 | |
| β-strand | 90-95 | 6 | 3 |
| β-strand | 100 | 1 | 4 |
| α-helix | 101-103 | 3 | |
| α-helix | 106-111 | 6 | |
| α-helix | 135-141 | 7 | |
| α-helix | 155-162 | 8 | |
| α-helix | 164-165 | 2 | |
| α-helix | 166-169 | 4 | |
| β-strand | 172-175 | 4 | 1 |
| β-strand | 178-179 | 2 | 1 |
| α-helix | 182-184 | 3 | |
| β-strand | 185-190 | 6 | 3 |
| β-strand | 193-198 | 6 | 3 |
| α-helix | 205-208 | 4 | |
| β-strand | 209-210 | 2 | 2 |
| α-helix | 215-217 | 3 | |
| β-strand | 219-224 | 6 | 1 |
| α-helix | 227-229 | 3 | |
| β-strand | 230 | 1 | 4 |
| α-helix | 231-233 | 3 | |
| β-strand | 244 | 1 | 5 |
| β-strand | 246-251 | 6 | 3 |
| α-helix | 259-262 | 4 | |
| β-strand | 264-266 | 3 | 3 |
| β-strand | 270-282 | 13 | 1 |
| β-strand | 292 | 1 | 6 |
| α-helix | 306-322 | 17 | |
| β-strand | 325 | 1 | 7 |
| α-helix | 333-334 | 2 | |
| β-strand | 335 | 1 | 7 |
| α-helix | 336-337 | 2 | |
| α-helix | 338-340 | 3 | |
| α-helix | 341-345 | 5 | |
| α-helix | 346-350 | 5 | |
| α-helix | 351-355 | 5 | |
| α-helix | 363-364 | 2 | |
| β-strand | 365 | 1 | 6 |
| β-strand | 368-379 | 12 | 1 |
| α-helix | 386-392 | 7 | |
| α-helix | 397-403 | 7 | |
| β-strand | 404-423 | 20 | 1 |
| α-helix | 427-441 | 15 | |
| α-helix | 448-461 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Acid-sensing ion channel 1 | A, B, C | protein | 527 | Gallus gallus | Q1XA76 (AlphaFold model) |
>6VTK_1 Acid-sensing ion channel 1 (chains A, B, C) MMDLKVDEEEVDSGQPVSIQAFASSSTLHGISHIFSYERLSLKRVVWALCFMGSLALLAL VCTNRIQYYFLYPHVTKLDEVAATRLTFPAVTFCNLNEFRFSRVTKNDLYHAGELLALLN NRYEIPDTQTADEKQLEILQDKANFRNFKPKPFNMLEFYDRAGHDIREMLLSCFFRGEQC SPEDFKVVFTRYGKCYTFNAGQDGKPRLITMKGGTGNGLEIMLDIQQDEYLPVWGETDET SFEAGIKVQIHSQDEPPLIDQLGFGVAPGFQTFVSCQEQRLIYLPPPWGDCKATTGDSEF YDTYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDNEYC VCEMPCNVTRYGKELSMVKIPSKASAKYLAKKYNKSEQYIGENILVLDIFFEALNYETIE QKKAYEVAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHRLCRRGKCRKNHKRNNTD KGVALSMDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 6 |
The His-Gly motif of acid-sensing ion channels resides in a reentrant 'loop' implicated in gating and ion selectivity. Yoder, N., Gouaux, E. Elife (2020) 9. DOI 10.7554/eLife.56527 · PubMed
Other PDB entries of the same protein (UniProt Q1XA76 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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