Poliovirus Polymerase Full Length Apo Structure. Determined by X-ray diffraction at 2.0 Å resolution. Released 17 Aug 2004.
Explore 1RA6 in 3D Show helices and sheets RCSB PDB PDBe
1RA6 contains 29 α-helices and 23 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 2-8 | 7 | 1 |
| α-helix | 15-18 | 4 | |
| β-strand | 26-27 | 2 | 2 |
| β-strand | 39-40 | 2 | 3 |
| α-helix | 41-42 | 2 | |
| α-helix | 54-59 | 6 | |
| α-helix | 72-86 | 15 | |
| α-helix | 97-102 | 6 | |
| β-strand | 104 | 1 | 4 |
| β-strand | 107 | 1 | 4 |
| α-helix | 108-111 | 4 | |
| α-helix | 127-130 | 4 | |
| α-helix | 139-147 | 9 | |
| α-helix | 152-153 | 2 | |
| β-strand | 154-158 | 5 | 1 |
| β-strand | 162-163 | 2 | 3 |
| α-helix | 165-169 | 5 | |
| β-strand | 175-178 | 4 | 1 |
| α-helix | 179-180 | 2 | |
| α-helix | 181-200 | 20 | |
| β-strand | 203 | 1 | 5 |
| β-strand | 208 | 1 | 5 |
| α-helix | 214-217 | 4 | |
| α-helix | 221-224 | 4 | |
| β-strand | 228-230 | 3 | 5 |
| β-strand | 233-234 | 2 | 6 |
| α-helix | 237-240 | 4 | |
| α-helix | 243-253 | 11 | |
| α-helix | 254-258 | 5 | |
| α-helix | 259-261 | 3 | |
| α-helix | 263-269 | 7 | |
| β-strand | 270-275 | 6 | 1 |
| β-strand | 278-283 | 6 | 1 |
| β-strand | 289 | 1 | 1 |
| α-helix | 293-312 | 20 | |
| α-helix | 318-320 | 3 | |
| β-strand | 322-326 | 5 | 5 |
| β-strand | 329-334 | 6 | 5 |
| α-helix | 340-349 | 10 | |
| β-strand | 354-355 | 2 | 6 |
| β-strand | 373 | 1 | 7 |
| β-strand | 376 | 1 | 7 |
| β-strand | 377-380 | 4 | 8 |
| β-strand | 388-391 | 4 | 8 |
| α-helix | 394-401 | 8 | |
| β-strand | 403-404 | 2 | 2 |
| α-helix | 407-409 | 3 | |
| α-helix | 410-421 | 12 | |
| α-helix | 422-424 | 3 | |
| α-helix | 426-436 | 11 | |
| α-helix | 440-443 | 4 | |
| α-helix | 450-460 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Genome polyprotein | A | protein | 461 | Human poliovirus 1 | P03300 (AlphaFold model) |
>1RA6_1 Genome polyprotein (chains A) GEIQWMRPSKEVGYPIINAPSKTKLEPSAFHYVFEGVKEPAVLTKNDPRLKTDFEEAIFS KYVGNKITEVDEYMKEAVDHYAGQLMSLDINTEQMCLEDAMYGTDGLEALDLSTSAGYPY VAMGKKKRDILNKQTRDTKEMQKLLDTYGINLPLVTYVKDELRSKTKVEQGKSRLIEASS LNDSVAMRMAFGNLYAAFHKNPGVITGSAVGCDPDLFWSKIPVLMEEKLFAFDYTGYDAS LSPAWFEALKMVLEKIGFGDRVDYIDYLNHSHHLYKNKTYCVKGGMPSGCSGTSIFNSMI NNLIIRTLLLKTYKGIDLDHLKMIAYGDDVIASYPHEVDASLLAQSGKDYGLTMTPADKS ATFETVTWENVTFLKRFFRADEKYPFLIHPVMPMKEIHESIRWTKDPRNTQDHVRSLCLL AWHNGEEEYNKFLAKIRSVPIGRALDLPEYSTLYDRWLDSF
Structural basis for proteolysis-dependent activation of the poliovirus RNA-dependent RNA polymerase. Thompson, A.A., Peersen, O.B. EMBO J (2004) 23:3462-3471. DOI 10.1038/sj.emboj.7600357 · PubMed
Other PDB entries of the same protein (UniProt P03300 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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