5F0M: Retromer VPS26-VPS35 subunits

Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1 (SeMet labeled). Determined by X-ray diffraction at 3.1 Å resolution. Released 7 Dec 2016.

Method
X-ray diffraction
Resolution
3.1 Å
Organism
Homo sapiens
Chains
4
Atoms
7,544
Mol. weight
114.4 kDa
Released
7 Dec 2016

Explore 5F0M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5F0M contains 49 α-helices and 33 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: 29 helices, 1 β-strand

ElementResiduesLengthSheet
α-helix14-3522
α-helix39-5012
α-helix51-544
α-helix60-8627
α-helix90-912
α-helix94-985
α-helix104-12118
α-helix123-1253
α-helix126-13611
α-helix137-1393
β-strand14011
α-helix143-15614
α-helix176-19621
α-helix206-21510
α-helix217-22812
α-helix235-2373
α-helix238-2425
α-helix243-25210
α-helix256-26914
α-helix272-2776
α-helix279-2879
α-helix295-31117
α-helix324-33815
α-helix344-36118
α-helix366-38217
α-helix393-40816
α-helix412-4176
α-helix423-4275
α-helix430-44617
α-helix454-46815
Chain B: 8 helices, 27 β-strands
ElementResiduesLengthSheet
β-strand12-1872
α-helix251
β-strand26-3053
α-helix32-343
β-strand36-4273
β-strand48-5692
β-strand5914
β-strand6114
β-strand6515
β-strand67-78123
α-helix82-843
β-strand86-96113
β-strand9915
β-strand105-11172
β-strand121-12223
β-strand126-137123
β-strand143-15193
β-strand15516
α-helix162-1632
β-strand164-17077
β-strand174-18077
β-strand184-18638
β-strand190-200117
β-strand204-217141
β-strand224-237141
β-strand245-25177
α-helix252-2554
α-helix257-2604
β-strand261-26441
β-strand268-280131
β-strand285-29281
β-strand293-29538
α-helix2961
β-strand29716
α-helix298-2992
Chain C: 10 helices, 3 β-strands
ElementResiduesLengthSheet
α-helix14-174
α-helix18-225
α-helix24-252
β-strand29-39119
β-strand46-55109
β-strand64-7079
α-helix71-8414
α-helix89-924
α-helix98-1003
α-helix108-1103
α-helix112-13019
α-helix133-1364
α-helix139-1468
Chain D: 2 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand554-55631
α-helix5571
β-strand558-55927
α-helix5601

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vacuolar protein sorting-associated protein 35Aprotein462Homo sapiensQ96QK1 (AlphaFold model)
Vacuolar protein sorting-associated protein 26ABprotein321Homo sapiensO75436 (AlphaFold model)
Sorting nexin-3Cprotein167Homo sapiensO60493 (AlphaFold model)
Natural resistance-associated macrophage protein 2Dprotein18Homo sapiensP49281 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5F0M_1 Vacuolar protein sorting-associated protein 35 (chains A)
GAMGSKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYM
AISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKD
ILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSMDFVLLNFA
EMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILE
QVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLAL
FAHREDGPGIPADIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDY
VDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKHFHPLFEYF
DYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQD
Sequence of entity 2 (B), FASTA
>5F0M_2 Vacuolar protein sorting-associated protein 26A (chains B)
MSFLGGFFGPICEIDIVLNDGETRKMAEMKTEDGKVEKHYLFYDGESVSGKVNLAFKQPG
KRLEHQGIRIEFVGQIELFNDKSNTHEFVNLVKELALPGELTQSRSYDFEFMQVEKPYES
YIGANVRLRYFLKVTIVRRLTDLVKEYDLIVHQLATYPDVNNSIKMEVGIEDCLHIEFEY
NKSKYHLKDVIVGKIYFLLVRIKIQHMELQLIKKEITGIGPSTTTETETIAKYEIMDGAP
VKGESIPIRLFLAGYDPTPTMRDVNKKFSVRYFLNLVLVDEEDRRYFKQQEIILWRKAPE
KLRKQRTNFHQRFESPESQAS
Sequence of entity 3 (C), FASTA
>5F0M_3 Sorting nexin-3 (chains C)
GAMGSMAETVADTRRLITKPQNLNDAYGPPSNFLEIDVSNPQTVGVGRGRFTTYEIRVKT
NLPIFKLKESTVRRRYSDFEWLRSELERESKVVVPPLPGKAFLRQLPFRGDDGIFDDNFI
EERKQGLEQFINKVAGHPLAQNERCLHMFLQDEIIDKSYTPSKIRHA
Sequence of entity 4 (D), FASTA
>5F0M_4 Natural resistance-associated macrophage protein 2 (chains D)
TAQPELYLLNTMSHHHHH

Primary citation

Structural Mechanism for Cargo Recognition by the Retromer Complex. Lucas, M., Gershlick, D.C., Vidaurrazaga, A. et al. Cell (2016) 167:1623-1635.e14. DOI 10.1016/j.cell.2016.10.056 · PubMed

Other PDB entries of the same protein (UniProt Q96QK1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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