6SKU: Legionella effector AnkX

Legionella effector AnkX in complex with human Rab1b. Determined by X-ray diffraction at 3.2 Å resolution. Released 10 Jun 2020.

Method
X-ray diffraction
Resolution
3.2 Å
Organisms
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513), Homo sapiens
Chains
2
Atoms
7,557
Mol. weight
110.88 kDa
Ligands
MG, GDP
Released
10 Jun 2020

Explore 6SKU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6SKU contains 63 α-helices and 19 β-strands across 2 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: 55 helices, 13 β-strands

ElementResiduesLengthSheet
α-helix12-165
α-helix19-213
α-helix23-253
α-helix29-324
α-helix39-446
α-helix48-6215
α-helix74-829
β-strand106-10831
α-helix111-1133
β-strand11412
α-helix116-1249
α-helix126-1316
β-strand135-13731
β-strand138-13923
β-strand146-14723
α-helix160-17415
β-strand181-18441
α-helix185-1862
α-helix190-20718
α-helix213-22816
α-helix235-2384
α-helix239-2435
α-helix244-2507
β-strand26612
α-helix269-29224
α-helix294-2963
α-helix305-3128
α-helix318-3214
α-helix334-34310
α-helix352-3598
α-helix363-3708
α-helix375-3784
α-helix382-3832
α-helix395-4017
α-helix405-4139
α-helix428-4347
α-helix438-45013
α-helix454-4585
β-strand46114
β-strand46714
α-helix468-4747
α-helix478-4858
β-strand49515
β-strand50115
α-helix502-5087
α-helix512-5209
α-helix523-5253
α-helix527-53610
α-helix539-54911
α-helix556-5649
α-helix568-57710
α-helix592-5987
α-helix602-6109
α-helix625-6284
α-helix629-6313
α-helix634-64714
α-helix662-6687
α-helix672-6809
α-helix695-6995
α-helix706-71510
α-helix728-7347
α-helix743-75715
α-helix758-7603
β-strand76616
β-strand77316
α-helix774-7818
α-helix787-7937
α-helix796-7994
Chain B: 8 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand8-1367
α-helix20-289
α-helix38-414
β-strand44-5077
β-strand55-6287
β-strand82-8877
α-helix92-965
α-helix98-1025
α-helix104-1085
β-strand114-12077
α-helix125-1273
α-helix132-14110
β-strand146-14837
α-helix157-17115

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phosphocholine transferase AnkXAprotein803Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)Q5ZXN6 (AlphaFold model)
Ras-related protein Rab-1BBprotein175Homo sapiensQ9H0U4 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>6SKU_1 Phosphocholine transferase AnkX (chains A)
GHMMVKIMPNLPGLYFLQAYPSEEIWRLFVDGRFWSKENGWRGYESREPGSLNAALESLC
SIALQVEKSGEEFELSVDLIKRIHKKSGKKVEELQEKNPGELRTDEPVSFCIPAGRASIK
GIEEFLSLVFLTEGGAEFGPGKAGPFGPRFDKNYFKNLNPEQIPDLAKQIYFDMSKYGHS
NTNHFYLAVMKNVDVYLEKITQSYNKEIKTAETLDEKLKIIVKHIRMYEVLHPFRDANGR
TFVNNLLNILLMQQGLPPATFYEPNVFDLYSAEELVVVVKEAIFNTVEIIEQSKRKTPIT
LYGYHSSLEEQTKFRDMLDSPSYEKIKHMDFSDLNPEKLHLKTQKCLSSLNEQYPLHRGA
IYLSDPGEIKLLLSNRNESQINQQIEQGAPPIYVGKTPAHLAVISGNMAMLDELIAKKAD
LSLQDYDGKTALHYAAECGNMQIMGKILKVVLSQEDAIKVLNIKDNHGKTAFHYAAEFGT
PELISALTTTEVIQINEPDNSGSSAITLAYKNHKLKIFDELLNSGADISDELLDAIWARK
DKETLGKIIAKNEKILLNKEAFRIAISLGSVSLVKKFLRAGVDIDIPLTKDKATPLMLSI
NSGNPKLVSYLLKKGANTRLTDTSGNSVLHYVFYSKAENREALANIITEKDKKLINQPNA
NGNPPLYNAVVVNDLKMATILLEMGARVDFEDRLGNNILHSAMRRCDLPIILDIVKKDST
LLHKRNSERRNPFHQALHEMHTFPSSKETEEIHFMNLSDLLLKEGVDLNKKDIKGKTILD
IALSKQYFHLCVKLMKAGAHTNI
Sequence of entity 2 (B), FASTA
>6SKU_2 Ras-related protein Rab-1B (chains B)
GPMPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKL
QIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLV
GNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKRMG

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg1
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21

Primary citation

Legionellaeffector AnkX displaces the switch II region for Rab1b phosphocholination. Ernst, S., Ecker, F., Kaspers, M.S. et al. Sci Adv (2020) 6:eaaz8041-eaaz8041. DOI 10.1126/sciadv.aaz8041 · PubMed

Other PDB entries of the same protein (UniProt Q5ZXN6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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