Structure of the Ebola virus nucleocapsid subunit. Determined by electron microscopy at 4.6 Å resolution. Released 29 Jan 2025.
Explore 8Y9J in 3D Show helices and sheets RCSB PDB PDBe
8Y9J contains 64 α-helices and 25 β-strands across 4 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 | 24-28 | 5 | |
| β-strand | 39-44 | 6 | 1 |
| α-helix | 49-63 | 15 | |
| α-helix | 69-83 | 15 | |
| α-helix | 86-90 | 5 | |
| α-helix | 94-101 | 8 | |
| β-strand | 104-109 | 6 | 1 |
| α-helix | 117-120 | 4 | |
| α-helix | 125-136 | 12 | |
| α-helix | 146-156 | 11 | |
| α-helix | 164-182 | 19 | |
| α-helix | 189-220 | 32 | |
| α-helix | 227-239 | 13 | |
| α-helix | 245-253 | 9 | |
| β-strand | 255-257 | 3 | 2 |
| β-strand | 262-264 | 3 | 2 |
| α-helix | 266-269 | 4 | |
| α-helix | 271-289 | 19 | |
| α-helix | 294-300 | 7 | |
| α-helix | 302-307 | 6 | |
| α-helix | 314-328 | 15 | |
| α-helix | 331-334 | 4 | |
| α-helix | 338-365 | 28 | |
| α-helix | 370-407 | 38 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 22-27 | 6 | |
| β-strand | 39-45 | 7 | 3 |
| α-helix | 49-63 | 15 | |
| α-helix | 67-82 | 16 | |
| α-helix | 86-92 | 7 | |
| α-helix | 94-102 | 9 | |
| β-strand | 104-110 | 7 | 3 |
| α-helix | 116-120 | 5 | |
| α-helix | 121-123 | 3 | |
| α-helix | 125-136 | 12 | |
| α-helix | 146-156 | 11 | |
| α-helix | 161-182 | 22 | |
| α-helix | 189-190 | 2 | |
| α-helix | 191-200 | 10 | |
| α-helix | 201-220 | 20 | |
| α-helix | 226-239 | 14 | |
| α-helix | 245-249 | 5 | |
| α-helix | 250-254 | 5 | |
| β-strand | 255-258 | 4 | 4 |
| β-strand | 261-264 | 4 | 4 |
| α-helix | 271-290 | 20 | |
| α-helix | 294-296 | 3 | |
| α-helix | 305-307 | 3 | |
| α-helix | 314-328 | 15 | |
| α-helix | 330-334 | 5 | |
| α-helix | 340-366 | 27 | |
| α-helix | 369-406 | 38 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-26 | 12 | |
| β-strand | 30-34 | 5 | 5 |
| β-strand | 37-42 | 6 | 5 |
| β-strand | 45-50 | 6 | 5 |
| α-helix | 52-61 | 10 | |
| α-helix | 67-75 | 9 | |
| α-helix | 77-80 | 4 | |
| β-strand | 86-87 | 2 | 6 |
| α-helix | 89-100 | 12 | |
| α-helix | 101-106 | 6 | |
| α-helix | 116-129 | 14 | |
| α-helix | 139-143 | 5 | |
| α-helix | 146-165 | 20 | |
| β-strand | 179-183 | 5 | 6 |
| β-strand | 186-191 | 6 | 6 |
| β-strand | 197-202 | 6 | 6 |
| α-helix | 205-209 | 5 | |
| β-strand | 218-222 | 5 | 6 |
| α-helix | 224-229 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 29-33 | 5 | 7 |
| β-strand | 37-42 | 6 | 7 |
| β-strand | 45-50 | 6 | 7 |
| α-helix | 54-60 | 7 | |
| α-helix | 67-81 | 15 | |
| β-strand | 87 | 1 | 8 |
| α-helix | 91-101 | 11 | |
| α-helix | 102-109 | 8 | |
| α-helix | 115-127 | 13 | |
| α-helix | 139-143 | 5 | |
| α-helix | 146-165 | 20 | |
| α-helix | 168-170 | 3 | |
| β-strand | 178-182 | 5 | 9 |
| β-strand | 187-193 | 7 | 9 |
| β-strand | 196-202 | 7 | 9 |
| α-helix | 207-210 | 4 | |
| β-strand | 218 | 1 | 9 |
| β-strand | 219 | 1 | 8 |
| α-helix | 224-229 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoprotein | A, B | protein | 739 | Zaire ebolavirus | P18272 (AlphaFold model) |
| Membrane-associated protein VP24 | C, D | protein | 251 | Zaire ebolavirus | Q05322 (AlphaFold model) |
| RNA (12-mer) | K | RNA | 12 | Homo sapiens |
>8Y9J_1 Nucleoprotein (chains A, B) MDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAF EAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEEL LPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHA EQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQAR FSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLL NLSGVNNLEHGLFPQLSAIALGVATAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAES RELDHLGLDDQEKKILMNFHQKKNEISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGH YDDDDDIPFPGPINDDDNPGHQDDDPTDSQDTTIPDVVVDPDDGSYGEYQSYSENGMNAP DDLVLFDLDEDDEDTKPVPNRSTKGGQQKNSQKGQHIEGRQTQSRPIQNVPGPHRTIHHA SAPLTDNDRRNEPSGSTSPRMLTPINEEADPLDDADDETSSLPPLESDDEEQDRDGTSNR TPTVAPPAPVYRDHSEKKELPQDEQQDQDHTQEARNQDSDNTQSEHSFEEMYRHILRSQG PFDAVLYYHMMKDEPVVFSTSDGKEYTYPDSLEEEYPPWLTEKEAMNEENRFVTLDGQQF YWPVMNHKNKFMAILQHHQ
>8Y9J_2 Membrane-associated protein VP24 (chains C, D) MAKATGRYNLISPKKDLEKGVVLSDLCNFLVSQTIQGWKVYWAGIEFDVTHKGMALLHRL KTNDFAPAWSMTRNLFPHLFQNPNSTIESPLWALRVILAAGIQDQLIDQSLIEPLAGALG LISDWLLTTNTNHFNMRTQRVKEQLSLKMLSLIRSNILKFINKLDALHVVNYNGLLSSIE IGTQNHTIIITRTNMGFLVELQEPDKSAMNRMKPGPAKFSLLHESTLKAFTQGSSTRMQS LILEFNSSLAI
>8Y9J_3 RNA (12-MER) (chains K) UUUUUUUUUUUU
Structural basis for Ebola virus nucleocapsid assembly and function regulated by VP24. Fujita-Fujiharu, Y., Hu, S., Hirabayashi, A. et al. Nat Commun (2025) 16:2171-2171. DOI 10.1038/s41467-025-57236-4 · 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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