Cryo-EM structure of DENV2 NS5 in complex with Stem Loop A (SLA). Determined by electron microscopy at 3.6 Å resolution. Released 23 Oct 2024.
Explore 9DTT in 3D Show helices and sheets RCSB PDB PDBe
9DTT contains 45 α-helices and 24 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 |
|---|---|---|---|
| α-helix | 11-17 | 7 | |
| α-helix | 22-29 | 8 | |
| β-strand | 34-36 | 3 | 1 |
| α-helix | 37 | 1 | |
| α-helix | 39-47 | 9 | |
| α-helix | 58-67 | 10 | |
| β-strand | 75-80 | 6 | 2 |
| α-helix | 86-92 | 7 | |
| β-strand | 97-103 | 7 | 2 |
| α-helix | 113-115 | 3 | |
| β-strand | 124-126 | 3 | 2 |
| α-helix | 132-134 | 3 | |
| α-helix | 136-137 | 2 | |
| β-strand | 142-145 | 4 | 2 |
| α-helix | 154-168 | 15 | |
| β-strand | 177-182 | 6 | 2 |
| α-helix | 188-198 | 11 | |
| β-strand | 204-206 | 3 | 2 |
| β-strand | 218-221 | 4 | 2 |
| α-helix | 229-241 | 13 | |
| β-strand | 251-253 | 3 | 1 |
| α-helix | 254-257 | 4 | |
| α-helix | 274-288 | 15 | |
| β-strand | 304-311 | 8 | 3 |
| α-helix | 317-319 | 3 | |
| β-strand | 320-321 | 2 | 4 |
| α-helix | 323-327 | 5 | |
| α-helix | 330-332 | 3 | |
| α-helix | 336-342 | 7 | |
| α-helix | 350-354 | 5 | |
| α-helix | 355-359 | 5 | |
| α-helix | 368-385 | 18 | |
| α-helix | 396-401 | 6 | |
| α-helix | 422-428 | 7 | |
| α-helix | 430-441 | 12 | |
| α-helix | 442-444 | 3 | |
| α-helix | 479-489 | 11 | |
| α-helix | 492-495 | 4 | |
| α-helix | 512-524 | 13 | |
| β-strand | 530-533 | 4 | 5 |
| β-strand | 535-536 | 2 | 6 |
| α-helix | 544-547 | 4 | |
| α-helix | 550-555 | 6 | |
| α-helix | 559-571 | 13 | |
| β-strand | 576-584 | 9 | 3 |
| β-strand | 587-595 | 9 | 3 |
| α-helix | 606-626 | 21 | |
| α-helix | 637-656 | 20 | |
| β-strand | 659-661 | 3 | 5 |
| β-strand | 664-667 | 4 | 5 |
| α-helix | 679-683 | 5 | |
| β-strand | 687-688 | 2 | 6 |
| α-helix | 696-697 | 2 | |
| β-strand | 699-700 | 2 | 5 |
| α-helix | 703-705 | 3 | |
| β-strand | 708 | 1 | 7 |
| β-strand | 711 | 1 | 7 |
| β-strand | 712-717 | 6 | 8 |
| β-strand | 723-728 | 6 | 8 |
| α-helix | 731-738 | 8 | |
| β-strand | 740-741 | 2 | 4 |
| α-helix | 749-765 | 17 | |
| α-helix | 771-782 | 12 | |
| α-helix | 802-804 | 3 | |
| α-helix | 809-814 | 6 | |
| α-helix | 815-819 | 5 | |
| α-helix | 841-846 | 6 | |
| α-helix | 854-861 | 8 | |
| α-helix | 863-874 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA-directed RNA polymerase NS5 | A | protein | 920 | dengue virus type 2 | P14340 |
| stem loop A | B | RNA | 70 | dengue virus type 2 |
>9DTT_1 RNA-directed RNA polymerase NS5 (chains A) MGSSHHHHHHSSGENLYFQGGTGNIGETLGEKWKSRLNALGKSEFQIYKKSGIQEVDRTL AKEGIKRGETDHHAVSRGSAKLRWFVERNMVTPEGKVVDLGCGRGGWSYYCGGLKNVREV KGLTKGGPGHEEPIPMSTYGWNLVRLQSGVDVFFTPPEKCDTLLCDIGESSPNPTVEAGR TLRVLNLVENWLNNNTQFCIKVLNPYMPSVIEKMEALQRKYGGALVRNPLSRNSTHEMYW VSNASGNIVSSVNMISRMLINRFTMRHKKATYEPDVDLGSGTRNIGIESEIPNLDIIGKR IEKIKQEHETSWHYDQDHPYKTWAYHGSYETKQTGSASSMVNGVVRLLTKPWDVVPMVTQ MAMTDTTPFGQQRVFKEKVDTRTQEPKEGTKKLMKITAEWLWKELGKKKTPRMCTREEFT RKVRSNAALGAIFTDENKWKSAREAVEDSRFWELVDKERNLHLEGKCETCVYNMMGKREK KLGEFGKAKGSRAIWYMWLGARFLEFEALGFLNEDHWFSRENSLSGVEGEGLHKLGYILR DVSKKEGGAMYADDTAGWDTRITLEDLKNEEMVTNHMEGEHKKLAEAIFKLTYQNKVVRV QRPTPRGTVMDIISRRDQRGSGQVGTYGLNTFTNMEAQLIRQMEGEGVFKSIQHLTVTEE IAVQNWLARVGRERLSRMAISGDDCVVKPLDDRFASALTALNDMGKVRKDIQQWEPSRGW NDWTQVPFCSHHFHELIMKDGRVLVVPCRNQDELIGRARISQGAGWSLRETACLGKSYAQ MWSLMYFHRRDLRLAANAICSAVPSHWVPTSRTTWSIHAKHEWMTTEDMLTVWNRVWIQE NPWMEDKTPVESWEEIPYLGKREDQWCGSLIGLTSRATWAKNIQTAINQVRSLIGNEEYT DYMPSMKRFRREEEEAGVLW
>9DTT_2 stem loop A (chains B) AGUUGUUAGUCUACGUGGACCGACAAAGACAGAUUCUUUGAGGGAGCUAAGCUCAACGUA GUUCUAACAG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
Structural Dynamics of the Dengue Virus Non-structural 5 (NS5) Interactions with Promoter Stem Loop A (SLA). Obi, J.O., Kihn, K.C., McQueen, L. et al. bioRxiv (2024). DOI 10.1101/2024.12.03.626708 · PubMed
Other PDB entries of the same protein (UniProt P14340), best resolution first:
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