3L28: Polymerase cofactor VP35
Crystal structure of Zaire Ebola VP35 interferon inhibitory domain K339A mutant. Determined by X-ray diffraction at 2.4 Å resolution. Released 26 Jan 2010.
- Method
- X-ray diffraction
- Resolution
- 2.4 Å
- Organism
- Zaire ebolavirus
- Chains
- 6
- Atoms
- 6,253
- Mol. weight
- 86.98 kDa
- Released
- 26 Jan 2010
Explore 3L28 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
3L28 contains 58 α-helices and 26 β-strands across 6 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.
Chain A: 10 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 221-230 | 10 | |
| α-helix | 238-252 | 15 | |
| α-helix | 256-268 | 13 | |
| α-helix | 273-283 | 11 | |
| α-helix | 285-288 | 4 | |
| α-helix | 291-293 | 3 | |
| β-strand | 294-296 | 3 | 1 |
| α-helix | 300-302 | 3 | |
| α-helix | 305-308 | 4 | |
| 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 |
Chain B: 10 helices, 5 β-strands
| 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 | |
| β-strand | 290 | 1 | 2 |
| α-helix | 291-293 | 3 | |
| β-strand | 294-296 | 3 | 3 |
| α-helix | 300-302 | 3 | |
| α-helix | 305-308 | 4 | |
| β-strand | 311-312 | 2 | 3 |
| α-helix | 313-315 | 3 | |
| α-helix | 320-322 | 3 | |
| β-strand | 324-329 | 6 | 3 |
| β-strand | 335-339 | 5 | 3 |
Chain C: 10 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 221-229 | 9 | |
| 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 | 4 |
| α-helix | 300-302 | 3 | |
| α-helix | 305-308 | 4 | |
| 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 |
Chain D: 10 helices, 4 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 221-230 | 10 | |
| α-helix | 238-252 | 15 | |
| α-helix | 256-268 | 13 | |
| α-helix | 273-283 | 11 | |
| α-helix | 286-289 | 4 | |
| α-helix | 290-293 | 4 | |
| β-strand | 294-297 | 4 | 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 | 324-330 | 7 | 5 |
| β-strand | 335-339 | 5 | 5 |
Chain E: 9 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 223-230 | 8 | |
| α-helix | 238-251 | 14 | |
| α-helix | 258-268 | 11 | |
| α-helix | 273-283 | 11 | |
| β-strand | 290 | 1 | 2 |
| α-helix | 291-293 | 3 | |
| β-strand | 294-296 | 3 | 6 |
| α-helix | 300-302 | 3 | |
| α-helix | 307-309 | 3 | |
| β-strand | 311-312 | 2 | 6 |
| α-helix | 313-315 | 3 | |
| α-helix | 320-322 | 3 | |
| β-strand | 324-329 | 6 | 6 |
| β-strand | 335-339 | 5 | 6 |
Chain F: 9 helices, 4 β-strands
| 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 | 7 |
| α-helix | 300-302 | 3 | |
| β-strand | 311-312 | 2 | 7 |
| α-helix | 313-315 | 3 | |
| α-helix | 320-322 | 3 | |
| β-strand | 324-329 | 6 | 7 |
| β-strand | 335-339 | 5 | 7 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Polymerase cofactor VP35 | A, B, C, D, E, F | protein | 129 | Zaire ebolavirus | Q05127 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>3L28_1 Polymerase cofactor VP35 (chains A, B, C, D, E, F)
GHMGKPDISAKDLRNIMYDHLPGFGTAFHQLVQVICKLGKDSNSLDIIHAEFQASLAEGD
SPQCALIQITKRVPIFQDAAPPVIHIRSRGDIPRACQKSLRPVPPSPKIDRGWVCVFQLQ
DGKTLGLAI
Primary citation
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:
- 3FKE 1.4 Å, Structure of the Ebola VP35 Interferon Inhibitory Domain
- 4IBG 1.41 Å, Ebola virus VP35 bound to small molecule
- 4IBI 1.47 Å, Ebola virus VP35 bound to small molecule
- 4IBJ 1.54 Å, Ebola virus VP35 bound to small molecule
- 3L29 1.7 Å, Crystal Structure of Zaire Ebola VP35 interferon inhibitory domain K319A/R322A mutant
- 4IBC 1.75 Å, Ebola virus VP35 bound to small molecule
- 4IBB 1.75 Å, Ebola virus VP35 bound to small molecule
- 4IBD 1.84 Å, Ebola virus VP35 bound to small molecule
- 4IBK 1.85 Å, Ebola virus VP35 bound to small molecule
- 4IJE 1.9 Å, Crystal structure of the Zaire ebolavirus VP35 interferon inhibitory domain…
- 3L27 1.95 Å, Crystal structure of Zaire Ebola VP35 interferon inhibitory domain R312A mutant
- 4IBE 1.95 Å, Ebola virus VP35 bound to small molecule
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