5YIK: Legionella effector with its substrate

Structure of a Legionella effector with its substrate. Determined by X-ray diffraction at 3.1 Å resolution. Released 30 May 2018.

Method
X-ray diffraction
Resolution
3.1 Å
Organisms
Legionella pneumophila, Homo sapiens
Chains
4
Atoms
9,381
Mol. weight
136.19 kDa
Released
30 May 2018

Explore 5YIK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 54 helices, 29 β-strands

ElementResiduesLengthSheet
α-helix238-24710
α-helix248-2525
α-helix255-2562
β-strand265-26731
β-strand270-27231
α-helix279-30123
α-helix306-3083
α-helix315-3173
α-helix320-33213
α-helix344-36421
α-helix366-3683
α-helix369-3735
α-helix377-38812
α-helix398-40811
α-helix409-4135
α-helix418-43013
α-helix435-45117
β-strand45912
β-strand46613
α-helix4671
β-strand468-46924
β-strand474-47634
β-strand477-47935
β-strand483-48425
β-strand48616
β-strand49716
β-strand499-50024
β-strand512-51325
α-helix5141
β-strand51513
α-helix516-5216
β-strand53612
α-helix545-5528
α-helix555-5628
α-helix564-57815
α-helix581-5866
α-helix595-5962
α-helix600-61415
α-helix616-6183
β-strand61917
β-strand624-62637
β-strand629-63137
α-helix633-64210
α-helix645-6495
α-helix654-66512
α-helix6691
β-strand670-67128
β-strand682-68328
α-helix684-69411
α-helix701-71414
α-helix716-72611
α-helix735-75521
β-strand763-76869
α-helix772-78716
α-helix798-80811
α-helix811-8144
β-strand818-82259
α-helix825-8262
α-helix827-8315
β-strand836-84169
β-strand849-85139
β-strand859110
β-strand862-86659
β-strand871-883139
β-strand889-899119
α-helix905-9062
α-helix913-93422
α-helix941-95212
α-helix953-9553
α-helix960-9645
α-helix965-9706
α-helix971-98212
α-helix987-9959
α-helix997-9982
α-helix999-10035
α-helix1010-104132
α-helix1045-10539
β-strand1058-1059211
β-strand1061111
α-helix1068-108114
α-helix1094-111421
α-helix1123-114927
α-helix1160-119031
Chain C: 1 helix, 5 β-strands
ElementResiduesLengthSheet
β-strand2-6512
β-strand12-16512
α-helix23-3311
β-strand42-45412
β-strand48-49212
β-strand66-70512
Chain D: 2 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand2-7610
β-strand12-16510
α-helix23-3412
β-strand41-45510
β-strand48-49210
α-helix50-512
β-strand66-71610
Chain F: 4 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand1-7713
β-strand12-17613
β-strand22114
α-helix23-3412
α-helix38-403
β-strand41-45513
β-strand48-49213
α-helix50-512
β-strand55114
α-helix56-594
β-strand66-71613

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
SdeAAprotein968Legionella pneumophilaQ6RCR0
ubiquitinC, D, Fprotein78Homo sapiensP0CG47 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5YIK_1 SdeA (chains A)
GFSLYTDDTVKAAAQYAYDNYLGKPYTGSVESAPANFGGRMVYRQHHGLSHTLRTMAYAE
LIVEEARKAKLRGETLGKFKDGRTIADVTPQELKKIMIAQAFFVAGRDDEASDAKNYQKY
HEQSRDAFLKYVKDNESTLIPDVFKDQEDVNFYARVIEDKSHDWESTPAHVLINQGHMVD
LVRVKQPPESFLQRYFSSMQRWIGSQATEAVFGIQRQFFHATYEVVAGFDSDNKEPHLVV
SGLGRYVIGEDGQPIREAPKKGQKEGDLKVFPQTYKLKENERLMRVDEFLKLPEIQNTFP
GSGKHLQGGMPGMNEMDYWNRLNSLNRARCENDVDFCLKQLQTAHDKAKIEPIKQAFQSS
KGKERRQPNVDEIAAARIIQQILANPDCIHDDHVLINGQKLEQQFFRDLLAKCEMAVVGS
LLNDTDIGNIDTLMRHEKDTEFHSTNPEAVPVKIGEYWINDQRINNSSGNITQKKHDLIF
LMQNDAWYFSRVNAIAQNRDKGSTFKEVLITTLMTPLTSKALVDTSQAKPPTRLFRGLNL
SEEFTKGLIDQANAMIANTTERLFTDHSPEAFKQIKLNDLSKMSGRTNASTTTEIKLVKE
TWDSNVIFEMLDPDGLLHSKQVGRHGEGTESEFSVYLPEDVALVPVKVTLDGKTQKGENR
YVFTFVAVKSPDFTPRHESGYAVEPFLRMQAAKLAEVKSSIEKAQRAPDLETIFNLQNEV
EAVQYSHLSTGYKNFLKNTVGPVLENSLSGLMESDTDTLSKALAAFPSDTQWSAFNFEEA
RQAKRQMDAIKQMVGNKVVLDALTQCQDALEKQNIAGALDALKKIPSEKEMGTIRRELRE
QIQSARQELESLQRAVVTPVVTDEKKVRERYDALIENTSKKITELETGKLPNLDAVKKGI
SNLSNLKQEVTVLRNEKIRMHVGTDKVDFSDVEKLEQQIQVIDTKLADAYLLEVTKQISA
LEHHHHHH
Sequence of entity 2 (C, D, F), FASTA
>5YIK_2 ubiquitin (chains C, D, F)
SHMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSD
YNIQKESTLHLVLRLRGG

Primary citation

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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