Crystal Structure of Zaire Ebola VP35 interferon inhibitory domain K319A/R322A mutant. Determined by X-ray diffraction at 1.7 Å resolution. Released 2 Feb 2010.
Explore 3L29 in 3D Show helices and sheets RCSB PDB PDBe
3L29 contains 21 α-helices and 8 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 |
|---|---|---|---|
| α-helix | 221-229 | 9 | |
| α-helix | 238-252 | 15 | |
| α-helix | 256-269 | 14 | |
| α-helix | 273-283 | 11 | |
| α-helix | 285-287 | 3 | |
| α-helix | 290-293 | 4 | |
| β-strand | 294-297 | 4 | 1 |
| α-helix | 300-302 | 3 | |
| α-helix | 305-310 | 6 | |
| β-strand | 311-312 | 2 | 1 |
| α-helix | 313-315 | 3 | |
| α-helix | 320-322 | 3 | |
| β-strand | 324-330 | 7 | 1 |
| β-strand | 335-339 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 215-220 | 6 | |
| α-helix | 221-231 | 11 | |
| α-helix | 238-252 | 15 | |
| α-helix | 256-268 | 13 | |
| α-helix | 273-283 | 11 | |
| α-helix | 285-287 | 3 | |
| α-helix | 290-293 | 4 | |
| β-strand | 294-296 | 3 | 2 |
| α-helix | 300-302 | 3 | |
| α-helix | 305-310 | 6 | |
| β-strand | 311-313 | 3 | 2 |
| α-helix | 314-315 | 2 | |
| α-helix | 320-322 | 3 | |
| β-strand | 324-329 | 6 | 2 |
| β-strand | 335-339 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Polymerase cofactor VP35 | A, B | protein | 129 | Zaire ebolavirus | Q05127 (AlphaFold model) |
>3L29_1 Polymerase cofactor VP35 (chains A, B) GHMGKPDISAKDLRNIMYDHLPGFGTAFHQLVQVICKLGKDSNSLDIIHAEFQASLAEGD SPQCALIQITKRVPIFQDAAPPVIHIRSRGDIPRACQKSLRPVPPSPAIDAGWVCVFQLQ DGKTLGLKI
Mutations abrogating VP35 interaction with double-stranded RNA render ebola virus avirulent in guinea pigs. Prins, K.C., Delpeut, S., Leung, D.W. et al. J Virol (2010) 84:3004-3015. DOI 10.1128/JVI.02459-09 · PubMed
Other PDB entries of the same protein (UniProt Q05127 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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