Myxococcus xanthus EncA 3xHis pore mutant with tetrahedral symmetry. Determined by electron microscopy at 2.71 Å resolution. Released 22 May 2024.
Explore 8V4Q in 3D Show helices and sheets RCSB PDB PDBe
8V4Q contains 29 α-helices and 43 β-strands across 3 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 | 14-31 | 18 | |
| α-helix | 34-36 | 3 | |
| β-strand | 40-41 | 2 | 1 |
| β-strand | 50-52 | 3 | 2 |
| β-strand | 82-84 | 3 | 2 |
| α-helix | 85-86 | 2 | |
| β-strand | 88-94 | 7 | 1 |
| α-helix | 96-105 | 10 | |
| α-helix | 107-110 | 4 | |
| α-helix | 112-131 | 20 | |
| β-strand | 133 | 1 | 3 |
| β-strand | 138 | 1 | 3 |
| β-strand | 148-150 | 3 | 4 |
| α-helix | 160-174 | 15 | |
| β-strand | 181-185 | 5 | 4 |
| α-helix | 187-192 | 6 | |
| α-helix | 204-209 | 6 | |
| β-strand | 215-218 | 4 | 4 |
| β-strand | 227-231 | 5 | 4 |
| β-strand | 237-249 | 13 | 1 |
| β-strand | 253 | 1 | 5 |
| β-strand | 256 | 1 | 5 |
| β-strand | 257-269 | 13 | 1 |
| α-helix | 272-274 | 3 | |
| β-strand | 275-278 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-29 | 16 | |
| α-helix | 34-36 | 3 | |
| β-strand | 40-41 | 2 | 6 |
| β-strand | 50-52 | 3 | 7 |
| β-strand | 82-84 | 3 | 7 |
| α-helix | 85-86 | 2 | |
| β-strand | 87-94 | 8 | 6 |
| α-helix | 96-105 | 10 | |
| α-helix | 108-110 | 3 | |
| α-helix | 112-131 | 20 | |
| β-strand | 133 | 1 | 8 |
| β-strand | 138 | 1 | 8 |
| β-strand | 148-150 | 3 | 9 |
| α-helix | 160-173 | 14 | |
| β-strand | 181-185 | 5 | 9 |
| α-helix | 187-192 | 6 | |
| α-helix | 204-209 | 6 | |
| β-strand | 216-218 | 3 | 9 |
| β-strand | 227-231 | 5 | 9 |
| β-strand | 237-249 | 13 | 6 |
| β-strand | 253 | 1 | 10 |
| β-strand | 256 | 1 | 10 |
| β-strand | 257-269 | 13 | 6 |
| α-helix | 272-274 | 3 | |
| β-strand | 275-278 | 4 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-29 | 16 | |
| α-helix | 34-36 | 3 | |
| β-strand | 40 | 1 | 11 |
| β-strand | 87-94 | 8 | 11 |
| α-helix | 96-105 | 10 | |
| α-helix | 108-110 | 3 | |
| α-helix | 112-131 | 20 | |
| β-strand | 133 | 1 | 12 |
| β-strand | 138 | 1 | 12 |
| β-strand | 148-150 | 3 | 13 |
| α-helix | 160-174 | 15 | |
| β-strand | 181-185 | 5 | 13 |
| α-helix | 187-192 | 6 | |
| α-helix | 204-211 | 8 | |
| β-strand | 215-218 | 4 | 13 |
| β-strand | 227-231 | 5 | 13 |
| β-strand | 237-249 | 13 | 11 |
| β-strand | 253 | 1 | 14 |
| β-strand | 256 | 1 | 14 |
| β-strand | 257-269 | 13 | 11 |
| α-helix | 272-274 | 3 | |
| β-strand | 275-278 | 4 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Type 1 encapsulin shell protein EncA | A, B, C | protein | 287 | Myxococcus xanthus DK 1622 | Q1D6H4 (AlphaFold model) |
>8V4Q_1 Type 1 encapsulin shell protein EncA (chains A, B, C) MPDFLGHAENPLREEEWARLNETVIQVARRSLVGRRILDIYGPLGAGVQTVPYDEFQGVS PGAVDIVGEQETAMVFTDARKFKTIPIIYKDFLLHWRDIEAARTHNMPLDVSAAAGAAAL CAQQEDELIFYGDARLGYEGLMTANGRLTVPLGDWTSPGGGFQAIVEATRKLNEQGHFGP YAVVLSPRLYSQLHRIYEHHHVLEIETIRQLASDGVYQSNRLRGESGVVVSTGRENMDLA VSMDMVAAYLGASRMNHPFRVLEALLLRIKHPDAICTLEGAGATERR
Point mutation in a virus-like capsid drives symmetry reduction to form tetrahedral cages. Szyszka, T.N., Andreas, M.P., Lie, F. et al. Proc Natl Acad Sci U S A (2024) 121:e2321260121-e2321260121. DOI 10.1073/pnas.2321260121 · PubMed
Other PDB entries of the same protein (UniProt Q1D6H4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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