Crystal structure of Zaire Ebola VP35 interferon inhibitory domain R312A mutant. Determined by X-ray diffraction at 1.95 Å resolution. Released 26 Jan 2010.
Explore 3L27 in 3D Show helices and sheets RCSB PDB PDBe
3L27 contains 39 α-helices and 18 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 | 221-231 | 11 | |
| 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 | 294-296 | 3 | 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 | 324-329 | 6 | 1 |
| β-strand | 335-339 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 221-231 | 11 | |
| α-helix | 238-252 | 15 | |
| α-helix | 256-269 | 14 | |
| α-helix | 273-283 | 11 | |
| α-helix | 285-287 | 3 | |
| β-strand | 290 | 1 | 2 |
| α-helix | 291-293 | 3 | |
| β-strand | 294-297 | 4 | 3 |
| α-helix | 300-302 | 3 | |
| α-helix | 305-310 | 6 | |
| β-strand | 311-312 | 2 | 3 |
| α-helix | 320-322 | 3 | |
| β-strand | 324-330 | 7 | 3 |
| β-strand | 335-339 | 5 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 221-231 | 11 | |
| α-helix | 238-252 | 15 | |
| α-helix | 256-269 | 14 | |
| α-helix | 273-283 | 11 | |
| α-helix | 285-287 | 3 | |
| β-strand | 290 | 1 | 2 |
| α-helix | 291-293 | 3 | |
| β-strand | 294-296 | 3 | 4 |
| α-helix | 300-302 | 3 | |
| α-helix | 305-307 | 3 | |
| β-strand | 311-312 | 2 | 4 |
| α-helix | 313-315 | 3 | |
| α-helix | 320-322 | 3 | |
| β-strand | 324-329 | 6 | 4 |
| β-strand | 335-339 | 5 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| 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 | 5 |
| α-helix | 300-302 | 3 | |
| α-helix | 305-307 | 3 | |
| β-strand | 311-312 | 2 | 5 |
| α-helix | 313-315 | 3 | |
| α-helix | 320-322 | 3 | |
| β-strand | 324-329 | 6 | 5 |
| β-strand | 335-339 | 5 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Polymerase cofactor VP35 | A, B, C, D | protein | 129 | Zaire ebolavirus | Q05127 (AlphaFold model) |
>3L27_1 Polymerase cofactor VP35 (chains A, B, C, D) GHMGKPDISAKDLRNIMYDHLPGFGTAFHQLVQVICKLGKDSNSLDIIHAEFQASLAEGD SPQCALIQITKRVPIFQDAAPPVIHIRSRGDIPRACQKSLAPVPPSPKIDRGWVCVFQLQ DGKTLGLKI
| ID | Name | Formula | Copies |
|---|---|---|---|
| PO4 | Phosphate ion | O4 P | 9 |
Water and common crystallization additives (K, NA, GOL, CL) are not listed.
Structural basis for dsRNA recognition and interferon antagonism by Ebola VP35. Leung, D.W., Prins, K.C., Borek, D.M. et al. Nat Struct Mol Biol (2010) 17:165-172. DOI 10.1038/nsmb.1765 · 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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