Cargo-loaded Myxococcus xanthus EncA encapsulin engineered pore mutant with T=3 icosahedral symmetry. Determined by electron microscopy at 3.14 Å resolution. Released 18 Sept 2024.
Explore 9B9Q in 3D Show helices and sheets RCSB PDB PDBe
9B9Q contains 33 α-helices and 34 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 | 39 | 1 | |
| β-strand | 40 | 1 | 1 |
| α-helix | 41-43 | 3 | |
| β-strand | 50-51 | 2 | 2 |
| α-helix | 75-77 | 3 | |
| β-strand | 83-84 | 2 | 2 |
| α-helix | 85-86 | 2 | |
| β-strand | 88-94 | 7 | 1 |
| α-helix | 96-103 | 8 | |
| α-helix | 107-110 | 4 | |
| α-helix | 112-130 | 19 | |
| α-helix | 160-174 | 15 | |
| β-strand | 181-185 | 5 | 3 |
| α-helix | 187-192 | 6 | |
| α-helix | 198-206 | 9 | |
| β-strand | 207-212 | 6 | 3 |
| β-strand | 221-225 | 5 | 3 |
| β-strand | 232-243 | 12 | 1 |
| β-strand | 251-262 | 12 | 1 |
| α-helix | 266-268 | 3 | |
| β-strand | 269-271 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-31 | 18 | |
| α-helix | 34-36 | 3 | |
| β-strand | 40-43 | 4 | 4 |
| β-strand | 50-51 | 2 | 5 |
| α-helix | 72-75 | 4 | |
| β-strand | 83-84 | 2 | 5 |
| α-helix | 85 | 1 | |
| β-strand | 88-94 | 7 | 4 |
| α-helix | 96-105 | 10 | |
| α-helix | 112-130 | 19 | |
| α-helix | 162-175 | 14 | |
| β-strand | 181-185 | 5 | 6 |
| α-helix | 187-195 | 9 | |
| α-helix | 198-206 | 9 | |
| β-strand | 210-212 | 3 | 6 |
| β-strand | 221-225 | 5 | 6 |
| β-strand | 231-243 | 13 | 4 |
| β-strand | 247 | 1 | 7 |
| β-strand | 250 | 1 | 7 |
| β-strand | 251-263 | 13 | 4 |
| α-helix | 266-268 | 3 | |
| β-strand | 269-271 | 3 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-31 | 18 | |
| α-helix | 34-36 | 3 | |
| β-strand | 42-43 | 2 | 8 |
| β-strand | 50-53 | 4 | 9 |
| α-helix | 73-75 | 3 | |
| β-strand | 81-84 | 4 | 9 |
| α-helix | 85-86 | 2 | |
| β-strand | 88-94 | 7 | 8 |
| α-helix | 96-105 | 10 | |
| α-helix | 107-110 | 4 | |
| α-helix | 112-130 | 19 | |
| α-helix | 160-173 | 14 | |
| β-strand | 181-185 | 5 | 10 |
| α-helix | 187-192 | 6 | |
| α-helix | 198-205 | 8 | |
| β-strand | 209-212 | 4 | 10 |
| β-strand | 221-225 | 5 | 10 |
| β-strand | 231-243 | 13 | 8 |
| β-strand | 247 | 1 | 11 |
| β-strand | 250 | 1 | 11 |
| β-strand | 251-263 | 13 | 8 |
| α-helix | 266-268 | 3 | |
| β-strand | 269-271 | 3 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Type 1 encapsulin shell protein EncA | A, B, C | protein | 281 | Myxococcus xanthus DK 1622 | Q1D6H4 (AlphaFold model) |
| Encapsulin nanocompartment cargo protein EncC | F, G, H | protein | 12 | Myxococcus xanthus DK 1622 | Q1D3Y8 (AlphaFold model) |
>9B9Q_1 Type 1 encapsulin shell protein EncA (chains A, B, C) MPDFLGHAENPLREEEWARLNETVIQVARRSLVGRRILDIYGPLGAGVQTVPYDEFQGVS PGAVDIVGEQETAMVFTDARKFKTIPIIYKDFLLHWRDIEAARTHNMPLDVSAAAGAAAL CAQQEDELIFYGDARLGYEGLMTANGRLTVPLGDWTSPGGGFQAIVEATRKLNEQGHFGP YAVVLSPRLYSQLHRGGEIETIRQLASDGVYQSNRLRGESGVVVSTGRENMDLAVSMDMV AAYLGASRMNHPFRVLEALLLRIKHPDAICTLEGAGATERR
>9B9Q_2 Encapsulin nanocompartment cargo protein EncC (chains F, G, H) PEKRLTVGSLRR
Pore Engineering as a General Strategy to Improve Protein-Based Enzyme Nanoreactor Performance. Kwon, S., Andreas, M.P., Giessen, T.W. ACS Nano (2024) 18:25740-25753. DOI 10.1021/acsnano.4c08186 · 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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