Crystal structure of Legionella effector protein sdeA (lpg2157) aa. 211-910. Determined by X-ray diffraction at 2.2 Å resolution. Released 18 Apr 2018.
Explore 6B7Q in 3D Show helices and sheets RCSB PDB PDBe
6B7Q contains 44 α-helices and 27 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 | 227-229 | 3 | |
| 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 | 315-317 | 3 | |
| α-helix | 320-332 | 13 | |
| α-helix | 344-363 | 20 | |
| α-helix | 366-373 | 8 | |
| α-helix | 377-388 | 12 | |
| α-helix | 391-393 | 3 | |
| α-helix | 398-409 | 12 | |
| α-helix | 410-413 | 4 | |
| α-helix | 418-433 | 16 | |
| α-helix | 435-451 | 17 | |
| β-strand | 459-460 | 2 | 2 |
| β-strand | 466 | 1 | 3 |
| α-helix | 467 | 1 | |
| β-strand | 469 | 1 | 4 |
| β-strand | 474 | 1 | 4 |
| β-strand | 475-476 | 2 | 5 |
| β-strand | 477-478 | 2 | 6 |
| β-strand | 484 | 1 | 6 |
| β-strand | 486 | 1 | 7 |
| α-helix | 489-490 | 2 | |
| α-helix | 496-497 | 2 | |
| β-strand | 498 | 1 | 7 |
| α-helix | 499 | 1 | |
| β-strand | 500-501 | 2 | 5 |
| α-helix | 505-507 | 3 | |
| β-strand | 512-513 | 2 | 6 |
| α-helix | 514 | 1 | |
| β-strand | 515 | 1 | 3 |
| α-helix | 516-521 | 6 | |
| α-helix | 523-526 | 4 | |
| β-strand | 535-536 | 2 | 2 |
| α-helix | 545-552 | 8 | |
| α-helix | 555-560 | 6 | |
| α-helix | 564-585 | 22 | |
| α-helix | 588-590 | 3 | |
| α-helix | 592-594 | 3 | |
| α-helix | 596-599 | 4 | |
| α-helix | 600-614 | 15 | |
| α-helix | 616-618 | 3 | |
| β-strand | 619-620 | 2 | 8 |
| β-strand | 623-625 | 3 | 8 |
| β-strand | 630-631 | 2 | 8 |
| α-helix | 633-642 | 10 | |
| α-helix | 645-650 | 6 | |
| α-helix | 654-666 | 13 | |
| β-strand | 671-672 | 2 | 9 |
| α-helix | 680-681 | 2 | |
| β-strand | 682-683 | 2 | 9 |
| α-helix | 684-695 | 12 | |
| α-helix | 701-714 | 14 | |
| α-helix | 716-726 | 11 | |
| α-helix | 735-755 | 21 | |
| α-helix | 758-761 | 4 | |
| β-strand | 763-768 | 6 | 10 |
| α-helix | 772-786 | 15 | |
| α-helix | 809-815 | 7 | |
| β-strand | 818-822 | 5 | 10 |
| α-helix | 825-826 | 2 | |
| α-helix | 827-831 | 5 | |
| β-strand | 836-841 | 6 | 10 |
| β-strand | 848-850 | 3 | 10 |
| β-strand | 862-866 | 5 | 10 |
| β-strand | 871-883 | 13 | 10 |
| β-strand | 889-899 | 11 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SdeA | A | protein | 705 | Legionella pneumophila | Q5ZTK4 (AlphaFold model) |
>6B7Q_1 SdeA (chains A) GKDTSPKEMSVKPTAPQDKSVPVWNGFSLYTDDTVKAAAQYAYDNYLGKPYTGSVESAPA NFGGRMVYRQHHGLSHTLRTMAYAELIVEEARKAKLRGETLGKFKDGRTIADVTPQELKK IMIAQAFFVAGRDDEASDAKNYQKYHEQSRDAFLKYVKDNESTLLPDVFKDQEDVNFYAR VIEDKSHDWESTPAHVLINQGHMVDLVRVKQPPESFLQRYFSSMQRWIGSQATEAVFGIQ RQFFHATYEVVAGFDSDNKEPHLVVSGLGRYVIGEDGQPIREAPKKGQKEGDLKVFPQTY KLKENERLMRVDEFLKLPEIQNTFPGSGKHLQGGMPGMNEMDYWNRLNSLNRARCENDVD FCLKQLQTAHDKAKIEPIKQAFQSSKGKERRQPNVDEIAAARIIQQILANPDCIHDDHVL INGQKLEQQFFRDLLAKCEMAVVGSLLNDTDIGNIDTLMRHEKDTEFHSTNPEAVPVKIG EYWINDQRINNSSGNITQKKHDLIFLMQNDAWYFSRVNAIAQNRDKGSTFKEVLITTLMT PLTSKALVDTSQAKPPTRLFRGLNLSEEFTKGLIDQANAMIANTTERLFTDHSPEAFKQI KLNDLSKMSGRTNASTTTEIKLVKETWDSNVIFEMLDPDGLLHSKQVGRHGEGTESEFSV YLPEDVALVPVKVTLDGKTQKGENRYVFTFVAVKSPDFTPRHESG
| ID | Name | Formula | Copies |
|---|---|---|---|
| HG | Mercury (II) ion | Hg | 10 |
Mechanism of phosphoribosyl-ubiquitination mediated by a single Legionella effector. Akturk, A., Wasilko, D.J., Wu, X. et al. Nature (2018) 557:729-733. DOI 10.1038/s41586-018-0147-6 · PubMed
Other PDB entries of the same protein (UniProt Q5ZTK4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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