Structure of the Legionella pneumophila effector RidL (1-866). Determined by X-ray diffraction at 3.0 Å resolution. Released 13 Dec 2017.
Explore 5OT4 in 3D Show helices and sheets RCSB PDB PDBe
5OT4 contains 210 α-helices and 24 β-strands across 4 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 | 12-25 | 14 | |
| α-helix | 30-45 | 16 | |
| α-helix | 51-59 | 9 | |
| α-helix | 62-68 | 7 | |
| α-helix | 104-120 | 17 | |
| α-helix | 125-133 | 9 | |
| α-helix | 136-145 | 10 | |
| β-strand | 149 | 1 | 1 |
| β-strand | 151 | 1 | 1 |
| α-helix | 161-164 | 4 | |
| β-strand | 165-166 | 2 | 2 |
| β-strand | 174-175 | 2 | 2 |
| α-helix | 184-205 | 22 | |
| α-helix | 209-217 | 9 | |
| α-helix | 221-231 | 11 | |
| α-helix | 238-240 | 3 | |
| α-helix | 245-272 | 28 | |
| α-helix | 276-281 | 6 | |
| α-helix | 283-286 | 4 | |
| α-helix | 291-296 | 6 | |
| α-helix | 300-305 | 6 | |
| α-helix | 311-328 | 18 | |
| α-helix | 335-338 | 4 | |
| α-helix | 343-350 | 8 | |
| α-helix | 360-364 | 5 | |
| α-helix | 370-384 | 15 | |
| α-helix | 394-403 | 10 | |
| α-helix | 407-416 | 10 | |
| α-helix | 430-449 | 20 | |
| α-helix | 455-457 | 3 | |
| α-helix | 458-465 | 8 | |
| α-helix | 469-477 | 9 | |
| α-helix | 480-486 | 7 | |
| α-helix | 491-497 | 7 | |
| α-helix | 505-519 | 15 | |
| α-helix | 524-531 | 8 | |
| α-helix | 536-537 | 2 | |
| α-helix | 541-556 | 16 | |
| α-helix | 564-578 | 15 | |
| α-helix | 583-589 | 7 | |
| α-helix | 604-613 | 10 | |
| α-helix | 618-625 | 8 | |
| α-helix | 631-639 | 9 | |
| α-helix | 649-656 | 8 | |
| α-helix | 665-673 | 9 | |
| α-helix | 680-692 | 13 | |
| α-helix | 695-711 | 17 | |
| α-helix | 715-741 | 27 | |
| α-helix | 743-750 | 8 | |
| α-helix | 766-804 | 39 | |
| α-helix | 820-862 | 43 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-25 | 14 | |
| α-helix | 30-45 | 16 | |
| α-helix | 51-59 | 9 | |
| α-helix | 62-68 | 7 | |
| α-helix | 70-73 | 4 | |
| α-helix | 85-90 | 6 | |
| α-helix | 104-120 | 17 | |
| α-helix | 125-133 | 9 | |
| α-helix | 136-145 | 10 | |
| β-strand | 149 | 1 | 3 |
| β-strand | 151 | 1 | 3 |
| β-strand | 155 | 1 | 4 |
| β-strand | 158 | 1 | 4 |
| α-helix | 161-164 | 4 | |
| β-strand | 165-166 | 2 | 5 |
| α-helix | 172-173 | 2 | |
| β-strand | 174-175 | 2 | 5 |
| α-helix | 184-205 | 22 | |
| α-helix | 209-216 | 8 | |
| α-helix | 221-230 | 10 | |
| α-helix | 235-240 | 6 | |
| α-helix | 245-265 | 21 | |
| α-helix | 267-271 | 5 | |
| α-helix | 276-281 | 6 | |
| α-helix | 283-287 | 5 | |
| α-helix | 291-297 | 7 | |
| α-helix | 300-303 | 4 | |
| α-helix | 308-310 | 3 | |
| α-helix | 311-328 | 18 | |
| α-helix | 335-339 | 5 | |
| α-helix | 343-351 | 9 | |
| α-helix | 361-363 | 3 | |
| α-helix | 370-384 | 15 | |
| β-strand | 389 | 1 | 6 |
| β-strand | 392 | 1 | 6 |
| α-helix | 394-403 | 10 | |
| α-helix | 407-416 | 10 | |
| α-helix | 429-449 | 21 | |
| α-helix | 455-457 | 3 | |
| α-helix | 458-465 | 8 | |
| α-helix | 469-477 | 9 | |
| α-helix | 480-485 | 6 | |
| α-helix | 491-498 | 8 | |
| α-helix | 505-518 | 14 | |
| α-helix | 524-531 | 8 | |
| α-helix | 541-555 | 15 | |
| α-helix | 564-578 | 15 | |
| α-helix | 583-589 | 7 | |
| β-strand | 592 | 1 | 7 |
| β-strand | 599 | 1 | 7 |
| α-helix | 604-625 | 22 | |
| α-helix | 629-640 | 12 | |
| α-helix | 646-648 | 3 | |
| α-helix | 649-656 | 8 | |
| α-helix | 665-673 | 9 | |
| α-helix | 680-692 | 13 | |
| α-helix | 695-710 | 16 | |
| α-helix | 715-741 | 27 | |
| α-helix | 743-750 | 8 | |
| α-helix | 770-772 | 3 | |
| α-helix | 774-804 | 31 | |
| α-helix | 806-807 | 2 | |
| α-helix | 820-857 | 38 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4 | 1 | |
| α-helix | 6 | 1 | |
| α-helix | 13-25 | 13 | |
| α-helix | 31-45 | 15 | |
| α-helix | 51-59 | 9 | |
| α-helix | 62-68 | 7 | |
| α-helix | 70-73 | 4 | |
| α-helix | 85-89 | 5 | |
| α-helix | 104-120 | 17 | |
| α-helix | 125-131 | 7 | |
| α-helix | 136-145 | 10 | |
| α-helix | 161-164 | 4 | |
| β-strand | 165-166 | 2 | 8 |
| β-strand | 174-175 | 2 | 8 |
| α-helix | 184-205 | 22 | |
| α-helix | 209-217 | 9 | |
| α-helix | 221-230 | 10 | |
| α-helix | 237-240 | 4 | |
| α-helix | 245-273 | 29 | |
| α-helix | 276-281 | 6 | |
| α-helix | 283-286 | 4 | |
| α-helix | 291-294 | 4 | |
| α-helix | 301-305 | 5 | |
| α-helix | 308-310 | 3 | |
| α-helix | 311-328 | 18 | |
| α-helix | 335-338 | 4 | |
| α-helix | 343-350 | 8 | |
| α-helix | 360-363 | 4 | |
| α-helix | 370-383 | 14 | |
| α-helix | 394-403 | 10 | |
| α-helix | 407-417 | 11 | |
| α-helix | 429-449 | 21 | |
| α-helix | 458-465 | 8 | |
| α-helix | 469-477 | 9 | |
| α-helix | 479-481 | 3 | |
| α-helix | 482-487 | 6 | |
| α-helix | 491-498 | 8 | |
| α-helix | 505-519 | 15 | |
| α-helix | 525-531 | 7 | |
| α-helix | 541-543 | 3 | |
| α-helix | 544-551 | 8 | |
| α-helix | 568-575 | 8 | |
| α-helix | 586-589 | 4 | |
| α-helix | 609-615 | 7 | |
| α-helix | 617-625 | 9 | |
| α-helix | 632-638 | 7 | |
| α-helix | 646-648 | 3 | |
| α-helix | 650-656 | 7 | |
| α-helix | 657-659 | 3 | |
| α-helix | 665-673 | 9 | |
| α-helix | 680-690 | 11 | |
| α-helix | 695-708 | 14 | |
| α-helix | 719-731 | 13 | |
| α-helix | 732-734 | 3 | |
| α-helix | 775-779 | 5 | |
| α-helix | 782-785 | 4 | |
| α-helix | 788-799 | 12 | |
| α-helix | 833-836 | 4 | |
| α-helix | 841-849 | 9 | |
| α-helix | 851-854 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-26 | 15 | |
| α-helix | 30-45 | 16 | |
| α-helix | 51-60 | 10 | |
| α-helix | 62-68 | 7 | |
| α-helix | 70-72 | 3 | |
| α-helix | 85-88 | 4 | |
| α-helix | 104-118 | 15 | |
| α-helix | 125-133 | 9 | |
| α-helix | 136-144 | 9 | |
| β-strand | 149 | 1 | 9 |
| β-strand | 151 | 1 | 9 |
| α-helix | 162-164 | 3 | |
| β-strand | 165-166 | 2 | 10 |
| β-strand | 174-175 | 2 | 10 |
| α-helix | 184-205 | 22 | |
| α-helix | 209-216 | 8 | |
| α-helix | 221-230 | 10 | |
| α-helix | 237-240 | 4 | |
| α-helix | 245-265 | 21 | |
| α-helix | 267-272 | 6 | |
| α-helix | 276-281 | 6 | |
| α-helix | 283-286 | 4 | |
| α-helix | 291-296 | 6 | |
| α-helix | 300-305 | 6 | |
| α-helix | 308-310 | 3 | |
| α-helix | 311-326 | 16 | |
| α-helix | 335-339 | 5 | |
| α-helix | 343-350 | 8 | |
| α-helix | 361-363 | 3 | |
| α-helix | 367-371 | 5 | |
| α-helix | 372-384 | 13 | |
| β-strand | 389 | 1 | 11 |
| β-strand | 392 | 1 | 11 |
| α-helix | 394-403 | 10 | |
| α-helix | 407-417 | 11 | |
| α-helix | 427-449 | 23 | |
| α-helix | 454-456 | 3 | |
| α-helix | 458-466 | 9 | |
| α-helix | 469-475 | 7 | |
| α-helix | 480-486 | 7 | |
| α-helix | 491-498 | 8 | |
| α-helix | 505-518 | 14 | |
| α-helix | 524-531 | 8 | |
| α-helix | 543-556 | 14 | |
| α-helix | 568-578 | 11 | |
| α-helix | 583-588 | 6 | |
| β-strand | 592 | 1 | 12 |
| β-strand | 599 | 1 | 12 |
| α-helix | 604-615 | 12 | |
| α-helix | 617-625 | 9 | |
| α-helix | 629-638 | 10 | |
| α-helix | 646-648 | 3 | |
| α-helix | 649-653 | 5 | |
| α-helix | 665-673 | 9 | |
| α-helix | 680-692 | 13 | |
| α-helix | 695-709 | 15 | |
| α-helix | 715-735 | 21 | |
| α-helix | 738-752 | 15 | |
| α-helix | 775-803 | 29 | |
| α-helix | 821-853 | 33 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Interaptin | A, B, C, D | protein | 901 | Legionella pneumophila | Q5ZT54 (AlphaFold model) |
>5OT4_1 Interaptin (chains A, B, C, D) SMILEEYIRMAKNKEFFDALEEIAESAKNDETLRNELAKVLDDILKTDPSDPEAFRKIVA EHQEFWDEHDPSLMEFNEGRFFGKSRKQYLKSDDFLNSTDPTYNFQKLHQFAAEQRVKLG LEKSDTDTLVAILKNNPEECRAYIESKKPGLGNFSEGNVHGWLKEEYTPTIPPKAINKST GVLSDEAIKRIKEQARDLLLLKLINSSGNTQLLKDLRDAMSKPEAERAANALGFPTEGNG VLFLSREVVDALEERVEKLEQEAAKRGFDSYVQSLSHNALLAKKNGLESTTAAGFKNSLD EPYKTYLPESEWERAQGVLGARYLQAVLSSGTQNLKDALNAKDANALITELKKPALLGPH DYIDKAVTEENLGSLKKNMMKSFINNIKDETNLKALDALKALDGAKNLDKFKEVLGKLGI TPADWVKDTDLKDMKQWARARQFELEINRVSSLGSGAHSKLMSTLTKLPVEKQREILAKP QQLRHLMNAYESHVAEHYLGKNASGIAELLTENKRLEGFRAIHNAEVARVLANFKPEITL NDKQVAAINQALTTANSNPNTYTQATDYKILIDAIKTQSGSVNQKDFYNAFNLNDDGRAF TSSTPRKDEMSKQQQHNQHIYAEYNSTSNSGNKKLLAVLLSIEKPVTFSKDIVNRFLRPL KDSETPQDYADTLFGENPTNPANKKFKDDLLRELTPTVFNEIKNDLRKQELLDTNPAHVM TAIKALSTELESIKGITGPIRTNADKLKFINDIDPVHLYNPTFQGTARSKAAQMKERYEG LSRDCGLVVDQLRRQVVALEGHLKSLPKEGEFKAAGLTLEQKAEIKKLRTDLEAELSAVR EDLDFYKKIQGKLETIVKEVDVAAKGKMHYYYNSEGIKRHPPVSRDQIPPLPNVPNPSLR S
Molecular mechanism for the subversion of the retromer coat by the Legionella effector RidL. Romano-Moreno, M., Rojas, A.L., Williamson, C.D. et al. Proc Natl Acad Sci U S A (2017) 114:E11151-E11160. DOI 10.1073/pnas.1715361115 · PubMed
Other PDB entries of the same protein (UniProt Q5ZT54 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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