Structure of a Legionella effector with its substrate. Determined by X-ray diffraction at 3.1 Å resolution. Released 30 May 2018.
Explore 5YIK in 3D Show helices and sheets RCSB PDB PDBe
5YIK contains 61 α-helices and 46 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 | 238-247 | 10 | |
| α-helix | 248-252 | 5 | |
| α-helix | 255-256 | 2 | |
| β-strand | 265-267 | 3 | 1 |
| β-strand | 270-272 | 3 | 1 |
| α-helix | 279-301 | 23 | |
| α-helix | 306-308 | 3 | |
| α-helix | 315-317 | 3 | |
| α-helix | 320-332 | 13 | |
| α-helix | 344-364 | 21 | |
| α-helix | 366-368 | 3 | |
| α-helix | 369-373 | 5 | |
| α-helix | 377-388 | 12 | |
| α-helix | 398-408 | 11 | |
| α-helix | 409-413 | 5 | |
| α-helix | 418-430 | 13 | |
| α-helix | 435-451 | 17 | |
| β-strand | 459 | 1 | 2 |
| β-strand | 466 | 1 | 3 |
| α-helix | 467 | 1 | |
| β-strand | 468-469 | 2 | 4 |
| β-strand | 474-476 | 3 | 4 |
| β-strand | 477-479 | 3 | 5 |
| β-strand | 483-484 | 2 | 5 |
| β-strand | 486 | 1 | 6 |
| β-strand | 497 | 1 | 6 |
| β-strand | 499-500 | 2 | 4 |
| β-strand | 512-513 | 2 | 5 |
| α-helix | 514 | 1 | |
| β-strand | 515 | 1 | 3 |
| α-helix | 516-521 | 6 | |
| β-strand | 536 | 1 | 2 |
| α-helix | 545-552 | 8 | |
| α-helix | 555-562 | 8 | |
| α-helix | 564-578 | 15 | |
| α-helix | 581-586 | 6 | |
| α-helix | 595-596 | 2 | |
| α-helix | 600-614 | 15 | |
| α-helix | 616-618 | 3 | |
| β-strand | 619 | 1 | 7 |
| β-strand | 624-626 | 3 | 7 |
| β-strand | 629-631 | 3 | 7 |
| α-helix | 633-642 | 10 | |
| α-helix | 645-649 | 5 | |
| α-helix | 654-665 | 12 | |
| α-helix | 669 | 1 | |
| β-strand | 670-671 | 2 | 8 |
| β-strand | 682-683 | 2 | 8 |
| α-helix | 684-694 | 11 | |
| α-helix | 701-714 | 14 | |
| α-helix | 716-726 | 11 | |
| α-helix | 735-755 | 21 | |
| β-strand | 763-768 | 6 | 9 |
| α-helix | 772-787 | 16 | |
| α-helix | 798-808 | 11 | |
| α-helix | 811-814 | 4 | |
| β-strand | 818-822 | 5 | 9 |
| α-helix | 825-826 | 2 | |
| α-helix | 827-831 | 5 | |
| β-strand | 836-841 | 6 | 9 |
| β-strand | 849-851 | 3 | 9 |
| β-strand | 859 | 1 | 10 |
| β-strand | 862-866 | 5 | 9 |
| β-strand | 871-883 | 13 | 9 |
| β-strand | 889-899 | 11 | 9 |
| α-helix | 905-906 | 2 | |
| α-helix | 913-934 | 22 | |
| α-helix | 941-952 | 12 | |
| α-helix | 953-955 | 3 | |
| α-helix | 960-964 | 5 | |
| α-helix | 965-970 | 6 | |
| α-helix | 971-982 | 12 | |
| α-helix | 987-995 | 9 | |
| α-helix | 997-998 | 2 | |
| α-helix | 999-1003 | 5 | |
| α-helix | 1010-1041 | 32 | |
| α-helix | 1045-1053 | 9 | |
| β-strand | 1058-1059 | 2 | 11 |
| β-strand | 1061 | 1 | 11 |
| α-helix | 1068-1081 | 14 | |
| α-helix | 1094-1114 | 21 | |
| α-helix | 1123-1149 | 27 | |
| α-helix | 1160-1190 | 31 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 12 |
| β-strand | 12-16 | 5 | 12 |
| α-helix | 23-33 | 11 | |
| β-strand | 42-45 | 4 | 12 |
| β-strand | 48-49 | 2 | 12 |
| β-strand | 66-70 | 5 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-7 | 6 | 10 |
| β-strand | 12-16 | 5 | 10 |
| α-helix | 23-34 | 12 | |
| β-strand | 41-45 | 5 | 10 |
| β-strand | 48-49 | 2 | 10 |
| α-helix | 50-51 | 2 | |
| β-strand | 66-71 | 6 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-7 | 7 | 13 |
| β-strand | 12-17 | 6 | 13 |
| β-strand | 22 | 1 | 14 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 13 |
| β-strand | 48-49 | 2 | 13 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 14 |
| α-helix | 56-59 | 4 | |
| β-strand | 66-71 | 6 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SdeA | A | protein | 968 | Legionella pneumophila | Q6RCR0 |
| ubiquitin | C, D, F | protein | 78 | Homo sapiens | P0CG47 (AlphaFold model) |
>5YIK_1 SdeA (chains A) GFSLYTDDTVKAAAQYAYDNYLGKPYTGSVESAPANFGGRMVYRQHHGLSHTLRTMAYAE LIVEEARKAKLRGETLGKFKDGRTIADVTPQELKKIMIAQAFFVAGRDDEASDAKNYQKY HEQSRDAFLKYVKDNESTLIPDVFKDQEDVNFYARVIEDKSHDWESTPAHVLINQGHMVD LVRVKQPPESFLQRYFSSMQRWIGSQATEAVFGIQRQFFHATYEVVAGFDSDNKEPHLVV SGLGRYVIGEDGQPIREAPKKGQKEGDLKVFPQTYKLKENERLMRVDEFLKLPEIQNTFP GSGKHLQGGMPGMNEMDYWNRLNSLNRARCENDVDFCLKQLQTAHDKAKIEPIKQAFQSS KGKERRQPNVDEIAAARIIQQILANPDCIHDDHVLINGQKLEQQFFRDLLAKCEMAVVGS LLNDTDIGNIDTLMRHEKDTEFHSTNPEAVPVKIGEYWINDQRINNSSGNITQKKHDLIF LMQNDAWYFSRVNAIAQNRDKGSTFKEVLITTLMTPLTSKALVDTSQAKPPTRLFRGLNL SEEFTKGLIDQANAMIANTTERLFTDHSPEAFKQIKLNDLSKMSGRTNASTTTEIKLVKE TWDSNVIFEMLDPDGLLHSKQVGRHGEGTESEFSVYLPEDVALVPVKVTLDGKTQKGENR YVFTFVAVKSPDFTPRHESGYAVEPFLRMQAAKLAEVKSSIEKAQRAPDLETIFNLQNEV EAVQYSHLSTGYKNFLKNTVGPVLENSLSGLMESDTDTLSKALAAFPSDTQWSAFNFEEA RQAKRQMDAIKQMVGNKVVLDALTQCQDALEKQNIAGALDALKKIPSEKEMGTIRRELRE QIQSARQELESLQRAVVTPVVTDEKKVRERYDALIENTSKKITELETGKLPNLDAVKKGI SNLSNLKQEVTVLRNEKIRMHVGTDKVDFSDVEKLEQQIQVIDTKLADAYLLEVTKQISA LEHHHHHH
>5YIK_2 ubiquitin (chains C, D, F) SHMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSD YNIQKESTLHLVLRLRGG
Structural basis of ubiquitin modification by the Legionella effector SdeA. Dong, Y., Mu, Y., Xie, Y. et al. Nature (2018) 557:674-678. DOI 10.1038/s41586-018-0146-7 · PubMed
Other PDB entries of the same protein (UniProt Q6RCR0), best resolution first:
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