Ebola virus VP24 structure. Determined by X-ray diffraction at 1.92 Å resolution. Released 19 Mar 2014.
Explore 4M0Q in 3D Show helices and sheets RCSB PDB PDBe
4M0Q contains 23 α-helices and 20 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 | 16-26 | 11 | |
| β-strand | 28 | 1 | 1 |
| β-strand | 30-33 | 4 | 2 |
| β-strand | 37-42 | 6 | 2 |
| β-strand | 45-50 | 6 | 2 |
| α-helix | 54-60 | 7 | |
| α-helix | 70-74 | 5 | |
| α-helix | 77-80 | 4 | |
| β-strand | 85-87 | 3 | 3 |
| α-helix | 90-102 | 13 | |
| α-helix | 103-107 | 5 | |
| α-helix | 116-128 | 13 | |
| β-strand | 133 | 1 | 1 |
| α-helix | 139-142 | 4 | |
| α-helix | 147-165 | 19 | |
| α-helix | 167-169 | 3 | |
| β-strand | 178-182 | 5 | 3 |
| β-strand | 187-193 | 7 | 3 |
| β-strand | 196-202 | 7 | 3 |
| α-helix | 207-209 | 3 | |
| β-strand | 217-222 | 6 | 3 |
| α-helix | 224-228 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-26 | 10 | |
| β-strand | 28 | 1 | 4 |
| β-strand | 30-33 | 4 | 5 |
| β-strand | 37-42 | 6 | 5 |
| β-strand | 45-50 | 6 | 5 |
| α-helix | 54-60 | 7 | |
| α-helix | 70-75 | 6 | |
| α-helix | 77-80 | 4 | |
| β-strand | 85-87 | 3 | 6 |
| α-helix | 90-104 | 15 | |
| α-helix | 114-128 | 15 | |
| β-strand | 133 | 1 | 4 |
| α-helix | 142-144 | 3 | |
| α-helix | 147-165 | 19 | |
| α-helix | 167-169 | 3 | |
| β-strand | 178-182 | 5 | 6 |
| β-strand | 187-193 | 7 | 6 |
| β-strand | 196-202 | 7 | 6 |
| α-helix | 207-209 | 3 | |
| β-strand | 217-222 | 6 | 6 |
| α-helix | 224-228 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Membrane-associated protein VP24 | A, B | protein | 230 | Zaire ebolavirus | Q05322 (AlphaFold model) |
>4M0Q_1 Membrane-associated protein VP24 (chains A, B) GHMISPKKDLEKGVVLSDLCNFLVSQTIQGWKVYWAGIEFDVTHKGMALLHRLKTNDFAP AWSMTRNLFPHLFQNPNSTIESPLWALRVILAAGIQDQLIDQSLIEPLAGALGLISDWLL TTNTNHFNMRTQRVKEQLSLKMLSLIRSNILKFINKLDALHVVNYNGLLSSIEIGTQNHT IIITRTNMGFLVELQEPDKSAMNRMKPGPAKFSLLHESTLKAFTQGSSTR
The Marburg Virus VP24 Protein Interacts with Keap1 to Activate the Cytoprotective Antioxidant Response Pathway. Edwards, M.R., Johnson, B., Mire, C.E. et al. Cell Rep (2014) 6:1017-1025. DOI 10.1016/j.celrep.2014.01.043 · PubMed
Other PDB entries of the same protein (UniProt Q05322 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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