Tse3 structure. Determined by X-ray diffraction at 1.49 Å resolution. Released 23 Apr 2014.
Explore 4M5E in 3D Show helices and sheets RCSB PDB PDBe
4M5E contains 34 α-helices and 4 β-strands across 1 chain. 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 | 3-12 | 10 | |
| α-helix | 23-35 | 13 | |
| α-helix | 39-48 | 10 | |
| α-helix | 51-58 | 8 | |
| α-helix | 62-75 | 14 | |
| α-helix | 80-90 | 11 | |
| α-helix | 91-93 | 3 | |
| α-helix | 101-103 | 3 | |
| α-helix | 108-125 | 18 | |
| α-helix | 130-132 | 3 | |
| α-helix | 134-137 | 4 | |
| α-helix | 147-150 | 4 | |
| α-helix | 154-156 | 3 | |
| α-helix | 158-161 | 4 | |
| α-helix | 162-169 | 8 | |
| α-helix | 173-178 | 6 | |
| α-helix | 186-191 | 6 | |
| α-helix | 195-207 | 13 | |
| β-strand | 209 | 1 | 1 |
| α-helix | 210 | 1 | |
| α-helix | 215-217 | 3 | |
| α-helix | 222-223 | 2 | |
| β-strand | 224 | 1 | 1 |
| α-helix | 225-236 | 12 | |
| α-helix | 240-252 | 13 | |
| α-helix | 256-267 | 12 | |
| β-strand | 275-276 | 2 | 2 |
| β-strand | 281-282 | 2 | 2 |
| α-helix | 283-288 | 6 | |
| α-helix | 298-303 | 6 | |
| α-helix | 306-313 | 8 | |
| α-helix | 316-335 | 20 | |
| α-helix | 339-341 | 3 | |
| α-helix | 343-348 | 6 | |
| α-helix | 355-358 | 4 | |
| α-helix | 361-363 | 3 | |
| α-helix | 366-377 | 12 | |
| α-helix | 389-405 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Uncharacterized protein | A | protein | 410 | Pseudomonas aeruginosa | Q9HYC5 (AlphaFold model) |
>4M5E_1 Uncharacterized protein (chains A) MTATSDLIESLISYSWDDWQVTRQEARRVIAAIRNDNVPDATIAALDKSGSLIKLFQRVG PPELARSLIASIAGRTTMQRYQARNALIRSLINNPLGTQTDNWIYFPTITFFDICADLAD AAGRLGFAAAGATGVASQAIQGPFSGVGATGVNPTDLPSIAFGDQLKLLNKDPATVTKYS NPLGDLGAYLSQLSPQDKLNQAQTLVGQPISTLFPDAYPGNPPSRAKVMSAAARKYDLTP QLIGAIILAEQRDQTRDEDAKDYQAAVSIKSANTSIGLGQVVVSTAIKYELFTDLLGQPV RRGLSRKAVATLLASDEFNIFATARYIRYVANLASQQDLRKLPKTRGAFPSIDLRAYAGN PRNWPRDNVRALASEYTSRPWDDNLSPGWPMFVDDAYATFLDLEHHHHHH
Water and common crystallization additives (GOL) are not listed.
Structural insights into the T6SS effector protein Tse3 and the Tse3-Tsi3 complex from Pseudomonas aeruginosa reveal a calcium-dependent membrane-binding mechanism. Lu, D., Shang, G., Zhang, H. et al. Mol Microbiol (2014) 92:1092-1112. DOI 10.1111/mmi.12616 · PubMed
Other PDB entries of the same protein (UniProt Q9HYC5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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