Client-bound structure of a DegP trimer within a 12mer cage. Determined by electron microscopy at 2.6 Å resolution. Released 23 Nov 2022.
Explore 8F0A in 3D Show helices and sheets RCSB PDB PDBe
8F0A contains 45 α-helices and 96 β-strands across 9 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 |
|---|---|---|---|
| β-strand | 29-31 | 3 | 3 |
| β-strand | 34-36 | 3 | 2 |
| α-helix | 38-48 | 11 | |
| β-strand | 52-53 | 2 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14 | 1 | 1 |
| α-helix | 16-19 | 4 | |
| α-helix | 23-25 | 3 | |
| β-strand | 26-34 | 9 | 2 |
| β-strand | 83-94 | 12 | 2 |
| β-strand | 99-103 | 5 | 2 |
| α-helix | 104-107 | 4 | |
| β-strand | 110-116 | 7 | 2 |
| β-strand | 122-131 | 10 | 2 |
| β-strand | 136-141 | 6 | 2 |
| α-helix | 149-151 | 3 | |
| β-strand | 152 | 1 | 3 |
| α-helix | 153 | 1 | |
| α-helix | 155-157 | 3 | |
| β-strand | 162 | 1 | 4 |
| β-strand | 163-168 | 6 | 3 |
| α-helix | 170-172 | 3 | |
| β-strand | 176-187 | 12 | 3 |
| β-strand | 198-201 | 4 | 3 |
| β-strand | 213-215 | 3 | 3 |
| β-strand | 221-229 | 9 | 3 |
| β-strand | 239-243 | 5 | 3 |
| α-helix | 244-257 | 14 | |
| β-strand | 263-264 | 2 | 5 |
| β-strand | 267-271 | 5 | 6 |
| α-helix | 274-279 | 6 | |
| β-strand | 288-293 | 6 | 6 |
| α-helix | 298-302 | 5 | |
| β-strand | 309-313 | 5 | 6 |
| β-strand | 316-317 | 2 | 6 |
| α-helix | 321-328 | 8 | |
| α-helix | 332 | 1 | |
| β-strand | 336-343 | 8 | 6 |
| β-strand | 346-353 | 8 | 6 |
| β-strand | 355-356 | 2 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 375-378 | 4 | 16 |
| β-strand | 385-389 | 5 | 16 |
| α-helix | 395-398 | 4 | |
| β-strand | 406-410 | 5 | 16 |
| β-strand | 413-414 | 2 | 16 |
| α-helix | 418-425 | 8 | |
| β-strand | 432-438 | 7 | 16 |
| β-strand | 441-447 | 7 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Periplasmic serine endoprotease DegP | A, B, C | protein | 348 | Escherichia coli (strain K12) | P0C0V0 (AlphaFold model) |
| Periplasmic serine endoprotease DegP | D, E, F | protein | 75 | Escherichia coli (strain K12) | P0C0V0 (AlphaFold model) |
| Telomeric repeat-binding factor 1 | a, b, c | protein | 27 | Homo sapiens | P54274 (AlphaFold model) |
>8F0A_1 Periplasmic serine endoprotease DegP (chains A, B, C) MPSLAPMLEKVMPSVVSINVEGSTTVNTPRMPRNFQQFFGDDSPFCQEGSPFQSSPFCQG GQGGNGGGQQQKFMALGSGVIIDADKGYVVTNNHVVDNATVIKVQLSDGRKFDAKMVGKD PRSDIALIQIQNPKNLTAIKMADSDALRVGDYTVAIGNPFGLGETVTSGIVSALGRSGLN AENYENFIQTDAAINRGNAGGALVNLNGELIGINTAILAPDGGNIGIGFAIPSNMVKNLT SQMVEYGQVKRGELGIMGTELNSELAKAMKVDAQRGAFVSQVLPNSSAAKAGIKAGDVIT SLNGKPISSFAALRAQVGTMPVGSKLTLGLLRDGKQVNVNLELQQSSQ
>8F0A_2 Periplasmic serine endoprotease DegP (chains D, E, F) AEMSNKGKDQGVVVNNVKTGTPAAQIGLKKGDVIIGANQQAVKNIAELRKVLDSKPSVLA LNIQRGDSTIYLLMQ
>8F0A_3 Telomeric repeat-binding factor 1 (chains a, b, c) SKILLHYKFNNRTSVMLKDRWRTMKKL
Flexible Client-Dependent Cages in the Assembly Landscape of the Periplasmic Protease-Chaperone DegP. Harkness, R.W., Ripstein, Z.A., Di Trani, J.M. et al. J Am Chem Soc (2023) 145:13015-13026. DOI 10.1021/jacs.2c11849 · PubMed
Other PDB entries of the same protein (UniProt P0C0V0 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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