CryoEM structure of Xenopus KCNQ1 channel. Determined by electron microscopy at 3.7 Å resolution. Released 7 Jun 2017.
Explore 5VMS in 3D Show helices and sheets RCSB PDB PDBe
5VMS contains 29 α-helices and 6 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 | 96-104 | 9 | |
| α-helix | 110-134 | 25 | |
| α-helix | 136-138 | 3 | |
| α-helix | 140-167 | 28 | |
| α-helix | 168-170 | 3 | |
| α-helix | 176-185 | 10 | |
| α-helix | 187-205 | 19 | |
| α-helix | 219-227 | 9 | |
| α-helix | 228-231 | 4 | |
| α-helix | 233-235 | 3 | |
| α-helix | 236-247 | 12 | |
| α-helix | 249-273 | 25 | |
| β-strand | 278 | 1 | 1 |
| β-strand | 284 | 1 | 1 |
| α-helix | 289-301 | 13 | |
| α-helix | 313-349 | 37 | |
| α-helix | 351-353 | 3 | |
| α-helix | 354-356 | 3 | |
| α-helix | 357-375 | 19 | |
| α-helix | 498-522 | 25 | |
| α-helix | 524-525 | 2 | |
| α-helix | 527-555 | 29 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-21 | 15 | |
| β-strand | 28 | 1 | 2 |
| α-helix | 30-40 | 11 | |
| α-helix | 46-56 | 11 | |
| β-strand | 64 | 1 | 2 |
| α-helix | 66-74 | 9 | |
| α-helix | 80-93 | 14 | |
| α-helix | 95-97 | 3 | |
| β-strand | 101 | 1 | 3 |
| α-helix | 103-112 | 10 | |
| α-helix | 119-129 | 11 | |
| β-strand | 137 | 1 | 3 |
| α-helix | 139-145 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Potassium voltage-gated channel subfamily KQT member 1 | A | protein | 548 | Xenopus laevis | P70057 (AlphaFold model) |
| Calmodulin | B | protein | 149 | Homo sapiens | P0DP23 (AlphaFold model) |
>5VMS_1 Potassium voltage-gated channel subfamily KQT member 1 (chains A) MATDPPRPTINLDPRVSIYSGRRPLLSRTNIQGRVYNFLERPTGWKCFVYHFTVFLIVLI CLIFSVLSTIQQYNNLATETLFWMEIVLVVFFGAEYVVRLWSAGCRSKYVGVWGRLRFAR KPISVIDLIVVVASVIVLCVGSNGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSVV FIHRQELITTLYIGFLGLIFSSYFVYLAEKDAIDSSGEYQFGSYADALWWGVVTVTTIGY GDKVPQTWIGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASLI QTAWRCYAAENPDSATWKIYIRKQSRNHHLMSPSPKPKKSAMVKKKKIRTERDEGSTDKM LNIPHITYDHVADDRKNDGYSVESYENTVRKPFGFLDPSTGPFIRTSSFTDDLDMEGDTL LTPITHISELKEHHRAAIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMVRI KELQRRLDQSLGKPSLFLSVSDKVKDKGINTIGSRLNRVEDKVTQMDHKLNLITDMLHHL LTNQQSNS
>5VMS_2 Calmodulin (chains B) MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 3 |
Cryo-EM Structure of a KCNQ1/CaM Complex Reveals Insights into Congenital Long QT Syndrome. Sun, J., MacKinnon, R. Cell (2017) 169:1042-1050.e9. DOI 10.1016/j.cell.2017.05.019 · PubMed
Other PDB entries of the same protein (UniProt P70057 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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