Ebola nucleoprotein nucleocapsid-like assembly and the asymmetric unit. Determined by electron microscopy at 5.8 Å resolution. Released 7 Mar 2018.
Explore 6C54 in 3D Show helices and sheets RCSB PDB PDBe
6C54 contains 44 α-helices and 10 β-strands across 2 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 | 40-45 | 6 | 1 |
| α-helix | 49-62 | 14 | |
| α-helix | 69-73 | 5 | |
| α-helix | 75-80 | 6 | |
| α-helix | 87-91 | 5 | |
| α-helix | 94-100 | 7 | |
| β-strand | 105-110 | 6 | 1 |
| α-helix | 128-136 | 9 | |
| α-helix | 147-155 | 9 | |
| α-helix | 158-160 | 3 | |
| α-helix | 165-181 | 17 | |
| α-helix | 194-206 | 13 | |
| α-helix | 209-215 | 7 | |
| α-helix | 216-220 | 5 | |
| α-helix | 227-238 | 12 | |
| α-helix | 245-253 | 9 | |
| β-strand | 256 | 1 | 2 |
| β-strand | 263 | 1 | 2 |
| α-helix | 271-273 | 3 | |
| α-helix | 274-287 | 14 | |
| α-helix | 294-296 | 3 | |
| α-helix | 297-300 | 4 | |
| α-helix | 303-306 | 4 | |
| α-helix | 316-326 | 11 | |
| α-helix | 341-362 | 22 | |
| α-helix | 370-382 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 42 | 1 | |
| β-strand | 43-45 | 3 | 3 |
| α-helix | 49-62 | 14 | |
| α-helix | 69-77 | 9 | |
| α-helix | 78-82 | 5 | |
| α-helix | 87-91 | 5 | |
| α-helix | 94-100 | 7 | |
| β-strand | 108-110 | 3 | 3 |
| β-strand | 114 | 1 | 4 |
| β-strand | 116 | 1 | 4 |
| α-helix | 117-119 | 3 | |
| α-helix | 127-136 | 10 | |
| α-helix | 147-155 | 9 | |
| α-helix | 158-160 | 3 | |
| α-helix | 165-182 | 18 | |
| α-helix | 194-206 | 13 | |
| α-helix | 208-219 | 12 | |
| α-helix | 227-238 | 12 | |
| α-helix | 245-253 | 9 | |
| β-strand | 255-258 | 4 | 5 |
| β-strand | 261-264 | 4 | 5 |
| α-helix | 274-287 | 14 | |
| α-helix | 288-293 | 6 | |
| α-helix | 304-307 | 4 | |
| α-helix | 316-326 | 11 | |
| α-helix | 341-365 | 25 | |
| α-helix | 370-383 | 14 | |
| α-helix | 393-410 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoprotein | A, B | protein | 433 | Zaire ebolavirus | P18272 (AlphaFold model) |
>6C54_1 Nucleoprotein (chains A, B) LTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQ GDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTE ANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLM RTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRL HPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIALGVA TAHGSTLAGVNVGEQYQQLREAATEAEKQLQQYAESRELDHLGLDDQEKKILMNFHQKKN EISFQQTNAMVTLRKERLAKLTEAITAASLPKTSGHYDDDDDIPFPGPINDDDNPGHQDD DPTDSQDTTIPDV
Electron Cryo-microscopy Structure of Ebola Virus Nucleoprotein Reveals a Mechanism for Nucleocapsid-like Assembly. Su, Z., Wu, C., Shi, L. et al. Cell (2018) 172:966-978.e12. DOI 10.1016/j.cell.2018.02.009 · 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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