Structure of VPS35 N terminal region. Determined by X-ray diffraction at 3.07 Å resolution. Released 7 Dec 2016.
Explore 5F0K in 3D Show helices and sheets RCSB PDB PDBe
5F0K contains 141 α-helices and 0 β-strands across 5 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 | 13-35 | 23 | |
| α-helix | 39-50 | 12 | |
| α-helix | 51-54 | 4 | |
| α-helix | 60-85 | 26 | |
| α-helix | 91-98 | 8 | |
| α-helix | 104-120 | 17 | |
| α-helix | 123-125 | 3 | |
| α-helix | 126-136 | 11 | |
| α-helix | 137-139 | 3 | |
| α-helix | 143-156 | 14 | |
| α-helix | 176-196 | 21 | |
| α-helix | 211-228 | 18 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-242 | 5 | |
| α-helix | 243-251 | 9 | |
| α-helix | 256-269 | 14 | |
| α-helix | 272-275 | 4 | |
| α-helix | 279-287 | 9 | |
| α-helix | 295-310 | 16 | |
| α-helix | 324-338 | 15 | |
| α-helix | 344-360 | 17 | |
| α-helix | 366-381 | 16 | |
| α-helix | 392-408 | 17 | |
| α-helix | 412-415 | 4 | |
| α-helix | 421-425 | 5 | |
| α-helix | 430-443 | 14 | |
| α-helix | 456-468 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-36 | 25 | |
| α-helix | 39-49 | 11 | |
| α-helix | 50-54 | 5 | |
| α-helix | 60-84 | 25 | |
| α-helix | 90-97 | 8 | |
| α-helix | 98-100 | 3 | |
| α-helix | 104-119 | 16 | |
| α-helix | 123-125 | 3 | |
| α-helix | 126-137 | 12 | |
| α-helix | 143-156 | 14 | |
| α-helix | 176-196 | 21 | |
| α-helix | 197-199 | 3 | |
| α-helix | 206-213 | 8 | |
| α-helix | 214-216 | 3 | |
| α-helix | 217-228 | 12 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-242 | 5 | |
| α-helix | 243-251 | 9 | |
| α-helix | 256-269 | 14 | |
| α-helix | 272-276 | 5 | |
| α-helix | 279-283 | 5 | |
| α-helix | 285-288 | 4 | |
| α-helix | 295-308 | 14 | |
| α-helix | 324-336 | 13 | |
| α-helix | 344-361 | 18 | |
| α-helix | 366-380 | 15 | |
| α-helix | 392-408 | 17 | |
| α-helix | 415-417 | 3 | |
| α-helix | 421-425 | 5 | |
| α-helix | 430-442 | 13 | |
| α-helix | 458-467 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-35 | 23 | |
| α-helix | 39-50 | 12 | |
| α-helix | 51-54 | 4 | |
| α-helix | 60-84 | 25 | |
| α-helix | 89-97 | 9 | |
| α-helix | 98-100 | 3 | |
| α-helix | 104-121 | 18 | |
| α-helix | 123-125 | 3 | |
| α-helix | 126-136 | 11 | |
| α-helix | 137-139 | 3 | |
| α-helix | 143-157 | 15 | |
| α-helix | 158-160 | 3 | |
| α-helix | 176-196 | 21 | |
| α-helix | 210-213 | 4 | |
| α-helix | 217-229 | 13 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-242 | 5 | |
| α-helix | 243-252 | 10 | |
| α-helix | 256-269 | 14 | |
| α-helix | 272-275 | 4 | |
| α-helix | 279-288 | 10 | |
| α-helix | 295-310 | 16 | |
| α-helix | 324-338 | 15 | |
| α-helix | 344-361 | 18 | |
| α-helix | 366-383 | 18 | |
| α-helix | 394-408 | 15 | |
| α-helix | 415-417 | 3 | |
| α-helix | 432-443 | 12 | |
| α-helix | 456-468 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-35 | 22 | |
| α-helix | 39-50 | 12 | |
| α-helix | 51-54 | 4 | |
| α-helix | 60-84 | 25 | |
| α-helix | 90-99 | 10 | |
| α-helix | 104-121 | 18 | |
| α-helix | 123-125 | 3 | |
| α-helix | 126-136 | 11 | |
| α-helix | 137-139 | 3 | |
| α-helix | 143-156 | 14 | |
| α-helix | 176-196 | 21 | |
| α-helix | 209-215 | 7 | |
| α-helix | 217-228 | 12 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-242 | 5 | |
| α-helix | 243-253 | 11 | |
| α-helix | 256-269 | 14 | |
| α-helix | 272-276 | 5 | |
| α-helix | 279-288 | 10 | |
| α-helix | 295-307 | 13 | |
| α-helix | 324-337 | 14 | |
| α-helix | 344-360 | 17 | |
| α-helix | 366-380 | 15 | |
| α-helix | 394-403 | 10 | |
| α-helix | 423-425 | 3 | |
| α-helix | 430-444 | 15 | |
| α-helix | 456-467 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-35 | 23 | |
| α-helix | 39-49 | 11 | |
| α-helix | 50-54 | 5 | |
| α-helix | 60-84 | 25 | |
| α-helix | 91-98 | 8 | |
| α-helix | 104-119 | 16 | |
| α-helix | 123-125 | 3 | |
| α-helix | 126-136 | 11 | |
| α-helix | 137-139 | 3 | |
| α-helix | 143-157 | 15 | |
| α-helix | 176-199 | 24 | |
| α-helix | 206-215 | 10 | |
| α-helix | 217-227 | 11 | |
| α-helix | 235-237 | 3 | |
| α-helix | 238-242 | 5 | |
| α-helix | 243-253 | 11 | |
| α-helix | 256-269 | 14 | |
| α-helix | 272-276 | 5 | |
| α-helix | 279-288 | 10 | |
| α-helix | 295-311 | 17 | |
| α-helix | 324-338 | 15 | |
| α-helix | 344-361 | 18 | |
| α-helix | 367-380 | 14 | |
| α-helix | 392-406 | 15 | |
| α-helix | 414-416 | 3 | |
| α-helix | 435-443 | 9 | |
| α-helix | 455-468 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Vacuolar protein sorting-associated protein 35 | A, B, C, D, E | protein | 462 | Homo sapiens | Q96QK1 (AlphaFold model) |
>5F0K_1 Vacuolar protein sorting-associated protein 35 (chains A, B, C, D, E) GAMGSKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYM AISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKD ILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSMDFVLLNFA EMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILE QVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLAL FAHREDGPGIPADIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDY VDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKHFHPLFEYF DYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQD
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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