Intracellular cryo-tomography structure of EBOV nucleocapsid at 8.9 Angstrom. Determined by electron microscopy at 8.9 Å resolution. Released 2 Oct 2024.
Explore 8USN in 3D Show helices and sheets RCSB PDB PDBe
8USN contains 101 α-helices and 34 β-strands across 7 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 | 23-26 | 4 | |
| β-strand | 39-45 | 7 | 1 |
| α-helix | 49-60 | 12 | |
| α-helix | 67-82 | 16 | |
| α-helix | 87-90 | 4 | |
| α-helix | 94-100 | 7 | |
| β-strand | 104-110 | 7 | 1 |
| α-helix | 117-120 | 4 | |
| α-helix | 128-135 | 8 | |
| α-helix | 147-155 | 9 | |
| α-helix | 165-181 | 17 | |
| α-helix | 189-192 | 4 | |
| α-helix | 194-206 | 13 | |
| α-helix | 208-220 | 13 | |
| α-helix | 227-238 | 12 | |
| α-helix | 245-248 | 4 | |
| α-helix | 249-254 | 6 | |
| β-strand | 255-258 | 4 | 2 |
| β-strand | 261-264 | 4 | 2 |
| α-helix | 271-287 | 17 | |
| α-helix | 288-296 | 9 | |
| α-helix | 297-300 | 4 | |
| α-helix | 306-308 | 3 | |
| α-helix | 310-312 | 3 | |
| α-helix | 314-327 | 14 | |
| α-helix | 338-362 | 25 | |
| α-helix | 363-365 | 3 | |
| α-helix | 370-405 | 36 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 38 | 1 | |
| β-strand | 39-45 | 7 | 5 |
| α-helix | 49-62 | 14 | |
| α-helix | 72-82 | 11 | |
| α-helix | 87-91 | 5 | |
| α-helix | 94-100 | 7 | |
| β-strand | 104-110 | 7 | 5 |
| α-helix | 117-120 | 4 | |
| α-helix | 125-135 | 11 | |
| α-helix | 147-154 | 8 | |
| α-helix | 155-157 | 3 | |
| α-helix | 165-181 | 17 | |
| α-helix | 184-188 | 5 | |
| α-helix | 194-206 | 13 | |
| α-helix | 209-219 | 11 | |
| α-helix | 221-223 | 3 | |
| α-helix | 227-237 | 11 | |
| α-helix | 245-254 | 10 | |
| β-strand | 255-258 | 4 | 6 |
| β-strand | 261-264 | 4 | 6 |
| α-helix | 267-269 | 3 | |
| α-helix | 271-288 | 18 | |
| α-helix | 291-293 | 3 | |
| α-helix | 305-308 | 4 | |
| α-helix | 310-312 | 3 | |
| α-helix | 314-327 | 14 | |
| α-helix | 341-352 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 28-34 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-21 | 5 | |
| α-helix | 22-27 | 6 | |
| β-strand | 30-34 | 5 | 7 |
| β-strand | 37-42 | 6 | 7 |
| β-strand | 45-49 | 5 | 7 |
| α-helix | 54-61 | 8 | |
| α-helix | 67-75 | 9 | |
| β-strand | 86-87 | 2 | 8 |
| α-helix | 90-107 | 18 | |
| α-helix | 113-127 | 15 | |
| α-helix | 140-144 | 5 | |
| α-helix | 147-165 | 19 | |
| α-helix | 167-168 | 2 | |
| β-strand | 169 | 1 | 8 |
| α-helix | 170 | 1 | |
| β-strand | 179-182 | 4 | 8 |
| β-strand | 187-193 | 7 | 8 |
| β-strand | 196-201 | 6 | 8 |
| β-strand | 218-222 | 5 | 8 |
| α-helix | 224-230 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 222-231 | 10 | |
| α-helix | 238-253 | 16 | |
| α-helix | 256-268 | 13 | |
| α-helix | 273-281 | 9 | |
| α-helix | 291-293 | 3 | |
| β-strand | 294-297 | 4 | 11 |
| α-helix | 305-308 | 4 | |
| β-strand | 311-312 | 2 | 11 |
| α-helix | 320-322 | 3 | |
| β-strand | 324-330 | 7 | 11 |
| β-strand | 334-339 | 6 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoprotein | A, B, E | protein | 739 | Ebola virus - Mayinga, Zaire, 1976 | P18272 (AlphaFold model) |
| RNA (5'-r(*ap*ap*ap*ap*ap*a)-3') | C, D | RNA | 6 | Zaire | |
| Membrane-associated protein VP24 | I, J | protein | 251 | Ebola virus - Mayinga, Zaire, 1976 | Q05322 (AlphaFold model) |
| Polymerase cofactor VP35 | F, K | protein | 340 | Ebola virus - Mayinga, Zaire, 1976 | Q05127 (AlphaFold model) |
>8USN_1 Nucleoprotein (chains A, B, E) MDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAF EAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEEL LPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHA EQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQAR FSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLL NLSGVNNLEHGLFPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAES RELDHLGLDDQEKKILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGH YDDDDDIPFPGPINDDDNPGHQDDDPTDSQDTTIPDVVVDPDDGSYGEYQSYSENGMNAP DDLVLFDLDEDDEDTKPVPNRSTKGGQQKNSQKGQHIEGRQTQSRPIQNVPGPHRTIHHA SAPLTDNDRRNEPSGSTSPRMLTPINEEADPLDDADDETSSLPPLESDDEEQDRDGTSNR TPTVAPPAPVYRDHSEKKELPQDEQQDQDHTQEARNQDSDNTQSEHSFEEMYRHILRSQG PFDAVLYYHMMKDEPVVFSTSDGKEYTYPDSLEEEYPPWLTEKEAMNEENRFVTLDGQQF YWPVMNHKNKFMAILQHHQ
>8USN_2 RNA (5'-R(*AP*AP*AP*AP*AP*A)-3') (chains C, D) AAAAAA
>8USN_3 Membrane-associated protein VP24 (chains I, J) MAKATGRYNLISPKKDLEKGVVLSDLCNFLVSQTIQGWKVYWAGIEFDVTHKGMALLHRL KTNDFAPAWSMTRNLFPHLFQNPNSTIESPLWALRVILAAGIQDQLIDQSLIEPLAGALG LISDWLLTTNTNHFNMRTQRVKEQLSLKMLSLIRSNILKFINKLDALHVVNYNGLLSSIE IGTQNHTIIITRTNMGFLVELQEPDKSAMNRMKPGPAKFSLLHESTLKAFTQGSSTRMQS LILEFNSSLAI
>8USN_4 Polymerase cofactor VP35 (chains F, K) MTTRTKGRGHTAATTQNDRMPGPELSGWISEQLMTGRIPVSDIFCDIENNPGLCYASQMQ QTKPNPKTRNSQTQTDPICNHSFEEVVQTLASLATVVQQQTIASESLEQRITSLENGLKP VYDMAKTISSLNRVCAEMVAKYDLLVMTTGRATATAAATEAYWAEHGQPPPGPSLYEESA IRGKIESRDETVPQSVREAFNNLNSTTSLTEENFGKPDISAKDLRNIMYDHLPGFGTAFH QLVQVICKLGKDSNSLDIIHAEFQASLAEGDSPQCALIQITKRVPIFQDAAPPVIHIRSR GDIPRACQKSLRPVPPSPKIDRGWVCVFQLQDGKTLGLKI
Intracellular Ebola virus nucleocapsid assembly revealed by in situ cryo-electron tomography. Watanabe, R., Zyla, D., Parekh, D. et al. Cell (2024) 187:5587-5603.e19. DOI 10.1016/j.cell.2024.08.044 · PubMed
Other PDB entries of the same protein (UniProt P18272 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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