Crystal structures and functional analysis of murine norovirus RNA-dependent RNA polymerase. Determined by X-ray diffraction at 2.56 Å resolution. Released 8 Jun 2011.
Explore 3NAI in 3D Show helices and sheets RCSB PDB PDBe
3NAI contains 79 α-helices and 77 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 |
|---|---|---|---|
| β-strand | 11-12 | 2 | 1 |
| β-strand | 15-16 | 2 | 1 |
| β-strand | 17-20 | 4 | 2 |
| α-helix | 23-27 | 5 | |
| β-strand | 30-34 | 5 | 3 |
| α-helix | 39-40 | 2 | |
| β-strand | 46-47 | 2 | 4 |
| α-helix | 48-49 | 2 | |
| α-helix | 62-70 | 9 | |
| α-helix | 71-74 | 4 | |
| α-helix | 76-77 | 2 | |
| α-helix | 79-81 | 3 | |
| α-helix | 83-100 | 18 | |
| α-helix | 102-103 | 2 | |
| α-helix | 105-108 | 4 | |
| α-helix | 109-115 | 7 | |
| β-strand | 121 | 1 | 5 |
| β-strand | 129 | 1 | 5 |
| α-helix | 130-133 | 4 | |
| β-strand | 134 | 1 | 6 |
| β-strand | 139 | 1 | 6 |
| α-helix | 141-155 | 15 | |
| β-strand | 163-168 | 6 | 2 |
| β-strand | 172-173 | 2 | 4 |
| α-helix | 176-179 | 4 | |
| β-strand | 186-189 | 4 | 2 |
| α-helix | 192-210 | 19 | |
| β-strand | 218 | 1 | 7 |
| α-helix | 224-235 | 12 | |
| β-strand | 240-242 | 3 | 7 |
| β-strand | 245-246 | 2 | 8 |
| α-helix | 250-252 | 3 | |
| α-helix | 255-267 | 13 | |
| α-helix | 272-283 | 12 | |
| β-strand | 286-289 | 4 | 2 |
| β-strand | 293-297 | 5 | 2 |
| α-helix | 308-328 | 21 | |
| α-helix | 332-335 | 4 | |
| β-strand | 339-344 | 6 | 7 |
| β-strand | 347-352 | 6 | 7 |
| α-helix | 358-368 | 11 | |
| β-strand | 372-373 | 2 | 8 |
| α-helix | 382 | 1 | |
| β-strand | 385 | 1 | 7 |
| β-strand | 392-393 | 2 | 9 |
| β-strand | 396-400 | 5 | 9 |
| β-strand | 405-409 | 5 | 9 |
| α-helix | 411-419 | 9 | |
| β-strand | 420-426 | 7 | 3 |
| β-strand | 432 | 1 | 3 |
| α-helix | 441-451 | 11 | |
| α-helix | 455-470 | 16 | |
| α-helix | 481-489 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-12 | 2 | 10 |
| β-strand | 15-16 | 2 | 10 |
| β-strand | 17-20 | 4 | 11 |
| α-helix | 23-27 | 5 | |
| β-strand | 30-34 | 5 | 12 |
| α-helix | 39-41 | 3 | |
| β-strand | 46-47 | 2 | 13 |
| α-helix | 62-70 | 9 | |
| α-helix | 71-74 | 4 | |
| α-helix | 76-77 | 2 | |
| α-helix | 79-82 | 4 | |
| α-helix | 83-98 | 16 | |
| α-helix | 101-103 | 3 | |
| α-helix | 105-108 | 4 | |
| α-helix | 109-115 | 7 | |
| β-strand | 121 | 1 | 14 |
| β-strand | 129 | 1 | 14 |
| α-helix | 130-133 | 4 | |
| β-strand | 134 | 1 | 15 |
| β-strand | 139 | 1 | 15 |
| α-helix | 141-155 | 15 | |
| β-strand | 163-168 | 6 | 11 |
| β-strand | 172-173 | 2 | 13 |
| α-helix | 176-179 | 4 | |
| β-strand | 186-189 | 4 | 11 |
| α-helix | 192-210 | 19 | |
| β-strand | 218 | 1 | 16 |
| α-helix | 228-235 | 8 | |
| β-strand | 240-242 | 3 | 16 |
| β-strand | 245-246 | 2 | 17 |
| α-helix | 249-252 | 4 | |
| α-helix | 255-267 | 13 | |
| α-helix | 272-283 | 12 | |
| β-strand | 286-289 | 4 | 11 |
| β-strand | 293-297 | 5 | 11 |
| α-helix | 308-328 | 21 | |
| α-helix | 332-337 | 6 | |
| β-strand | 339-344 | 6 | 16 |
| β-strand | 347-352 | 6 | 16 |
| α-helix | 358-367 | 10 | |
| β-strand | 372-373 | 2 | 17 |
| α-helix | 382-383 | 2 | |
| β-strand | 385 | 1 | 16 |
| β-strand | 392-393 | 2 | 18 |
| β-strand | 396-401 | 6 | 18 |
| β-strand | 404-409 | 6 | 18 |
| α-helix | 411-419 | 9 | |
| β-strand | 420-426 | 7 | 12 |
| α-helix | 431 | 1 | |
| β-strand | 432 | 1 | 12 |
| α-helix | 433 | 1 | |
| α-helix | 441-451 | 11 | |
| α-helix | 454-469 | 16 | |
| α-helix | 481-489 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-12 | 2 | 19 |
| β-strand | 15-16 | 2 | 19 |
| β-strand | 17-20 | 4 | 20 |
| α-helix | 23-27 | 5 | |
| β-strand | 30-34 | 5 | 21 |
| α-helix | 39-41 | 3 | |
| β-strand | 46-47 | 2 | 22 |
| α-helix | 62-70 | 9 | |
| α-helix | 71-73 | 3 | |
| α-helix | 76-77 | 2 | |
| α-helix | 79-82 | 4 | |
| α-helix | 83-100 | 18 | |
| α-helix | 101-103 | 3 | |
| α-helix | 105-108 | 4 | |
| α-helix | 109-115 | 7 | |
| β-strand | 121 | 1 | 23 |
| β-strand | 129 | 1 | 23 |
| α-helix | 130-133 | 4 | |
| β-strand | 134 | 1 | 24 |
| β-strand | 139 | 1 | 24 |
| α-helix | 141-156 | 16 | |
| β-strand | 163-168 | 6 | 20 |
| β-strand | 172-173 | 2 | 22 |
| α-helix | 176-179 | 4 | |
| β-strand | 186-189 | 4 | 20 |
| α-helix | 192-210 | 19 | |
| β-strand | 218 | 1 | 25 |
| α-helix | 224-236 | 13 | |
| β-strand | 240-246 | 7 | 25 |
| α-helix | 255-267 | 13 | |
| α-helix | 272-283 | 12 | |
| β-strand | 286-289 | 4 | 20 |
| β-strand | 293-297 | 5 | 20 |
| α-helix | 308-328 | 21 | |
| α-helix | 332-337 | 6 | |
| β-strand | 339-344 | 6 | 25 |
| β-strand | 347-352 | 6 | 25 |
| α-helix | 358-367 | 10 | |
| β-strand | 372-374 | 3 | 25 |
| β-strand | 385 | 1 | 25 |
| β-strand | 392-393 | 2 | 26 |
| β-strand | 396-401 | 6 | 26 |
| β-strand | 404-409 | 6 | 26 |
| α-helix | 411-419 | 9 | |
| β-strand | 420-426 | 7 | 21 |
| β-strand | 432 | 1 | 21 |
| α-helix | 440-451 | 12 | |
| α-helix | 455-467 | 13 | |
| α-helix | 481-489 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA dependent RNA polymerase | A, B, C | protein | 517 | Murine norovirus 1 | Q80J95 (AlphaFold model) |
>3NAI_1 RNA dependent RNA polymerase (chains A, B, C) MLPRPSGTYAGLPIADYGDAPPLSTKTMFWRTSPEKLPPGAWEPAYLGSKDERVDGPSLQ QVMRDQLKPYSEPRGLLPPQEILDAVCDAIENRLENTLEPQKPWTFKKACESLDKNTSSG YPYHKQKSKDWTGSAFIGDLGDQATHANNMYEMGKSMRPIYTAALKDELVKPDKIYGKIK KRLLWGSDLGTMIRAARAFGPFCDALKETCIFNPIRVGMSMNEDGPFIFARHANFRYHMD ADYTRWDSTQQRAILKRAGDIMVRLSPEPDLARVVMDDLLAPSLLDVGDYKIVVEEGLPS GCPCTTQLNSLAHWILTLCAMVEVTRVDPDIVMQESEFSFYGDDEVVSTNLELDMVKYTM ALRRYGLLPTRADKEEGPLERRQTLQGISFLRRAIVGDQFGWYGRLDRASIDRQLLWTKG PNHQNPFETLPGHAQRPSQLMALLGEAAMHGEKYYRTVASRVSKEAAQSGIEMVVPRHRS VLRWVRFGTMDAETPQERSAVFVNEDAAALEHHHHHH
Water and common crystallization additives (GOL, SO4) are not listed.
Crystal structures and functional analysis of murine norovirus RNA-dependent RNA polymerase. Kim, K.H., Lee, J.H., Alam, I. et al. To be published.
Other PDB entries of the same protein (UniProt Q80J95 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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