Structure of Sortilin ECD in complex with TNFa-targeting SORTAC. Determined by X-ray diffraction at 2.8 Å resolution. Released 8 Apr 2026.
Explore 9R18 in 3D Show helices and sheets RCSB PDB PDBe
9R18 contains 16 α-helices and 59 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 | 92-97 | 6 | |
| β-strand | 100-105 | 6 | 1 |
| β-strand | 111-117 | 7 | 2 |
| β-strand | 123-133 | 11 | 2 |
| β-strand | 138-147 | 10 | 2 |
| β-strand | 154-156 | 3 | 2 |
| α-helix | 158-161 | 4 | |
| β-strand | 166 | 1 | 3 |
| β-strand | 182-186 | 5 | 3 |
| β-strand | 196-200 | 5 | 3 |
| β-strand | 208-211 | 4 | 3 |
| β-strand | 216 | 1 | 4 |
| β-strand | 221-222 | 2 | 5 |
| β-strand | 230-233 | 4 | 5 |
| β-strand | 234 | 1 | 4 |
| β-strand | 239-242 | 4 | 5 |
| β-strand | 250-251 | 2 | 5 |
| β-strand | 259-262 | 4 | 6 |
| β-strand | 266-271 | 6 | 6 |
| β-strand | 284 | 1 | 7 |
| β-strand | 285-289 | 5 | 6 |
| β-strand | 297-298 | 2 | 6 |
| β-strand | 303-309 | 7 | 7 |
| β-strand | 312-318 | 7 | 7 |
| α-helix | 319 | 1 | |
| β-strand | 325-330 | 6 | 7 |
| β-strand | 338-339 | 2 | 7 |
| β-strand | 345 | 1 | 7 |
| β-strand | 351-356 | 6 | 8 |
| β-strand | 361-366 | 6 | 8 |
| α-helix | 367 | 1 | |
| β-strand | 373-379 | 7 | 8 |
| β-strand | 386-394 | 9 | 8 |
| β-strand | 405 | 1 | 8 |
| β-strand | 414-419 | 6 | 8 |
| β-strand | 425-430 | 6 | 8 |
| β-strand | 437-439 | 3 | 8 |
| α-helix | 440-443 | 4 | |
| β-strand | 459-462 | 4 | 9 |
| α-helix | 465-469 | 5 | |
| β-strand | 479 | 1 | 9 |
| β-strand | 488-495 | 8 | 9 |
| β-strand | 504-508 | 5 | 9 |
| β-strand | 516-519 | 4 | 9 |
| β-strand | 523-528 | 6 | 10 |
| α-helix | 529-531 | 3 | |
| β-strand | 533-538 | 6 | 10 |
| β-strand | 544 | 1 | 11 |
| β-strand | 546-550 | 5 | 10 |
| β-strand | 558-561 | 4 | 10 |
| β-strand | 567 | 1 | 11 |
| β-strand | 568-574 | 7 | 1 |
| β-strand | 582-589 | 8 | 1 |
| β-strand | 596-603 | 8 | 1 |
| β-strand | 611 | 1 | 12 |
| α-helix | 612 | 1 | |
| α-helix | 614-616 | 3 | |
| β-strand | 617-621 | 5 | 13 |
| β-strand | 635 | 1 | 13 |
| β-strand | 638-645 | 8 | 13 |
| β-strand | 652 | 1 | 12 |
| β-strand | 660-665 | 6 | 13 |
| α-helix | 670-672 | 3 | |
| β-strand | 673-674 | 2 | 14 |
| β-strand | 679-680 | 2 | 15 |
| β-strand | 689-690 | 2 | 15 |
| α-helix | 691 | 1 | |
| α-helix | 697-704 | 8 | |
| α-helix | 707-710 | 4 | |
| β-strand | 711-712 | 2 | 16 |
| β-strand | 716-717 | 2 | 14 |
| α-helix | 718 | 1 | |
| α-helix | 731-733 | 3 | |
| β-strand | 734-735 | 2 | 16 |
| α-helix | 737-741 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sortilin | A | protein | 762 | Homo sapiens | Q99523 (AlphaFold model) |
>9R18_1 Sortilin (chains A) MERPWGAADGLSRWPHGLGLLLLLQLLPPSTLSQDRLDAPPPPAAPLPRWSGPIGVSWGL RAAAAGGAFPRGGRWRRSAPGEDEECGRVRDFVAKLANNTHQHVFDDLRGSVSLSWVGDS TGVILVLTTFHVPLVIMTFGQSKLYRSEDYGKNFKDITDLINNTFIRTEFGMAIGPENSG KVVLTAEVSGGSRGGRIFRSSDFAKNFVQTDLPFHPLTQMMYSPQNSDYLLALSTENGLW VSKNFGGKWEEIHKAVCLAKWGSDNTIFFTTYANGSCKADLGALELWRTSDLGKSFKTIG VKIYSFGLGGRFLFASVMADKDTTRRIHVSTDQGDTWSMAQLPSVGQEQFYSILAANDDM VFMHVDEPGDTGFGTIFTSDDRGIVYSKSLDRHLYTTTGGETDFTNVTSLRGVYITSVLS EDNSIQTMITFDQGGRWTHLRKPENSECDATAKNKNECSLHIHASYSISQKLNVPMAPLS EPNAVGIVIAHGSVGDAISVMVPDVYISDDGGYSWTKMLEGPHYYTILDSGGIIVAIEHS SRPINVIKFSTDEGQCWQTYTFTRDPIYFTGLASEPGARSMNISIWGFTESFLTSQWVSY TIDFKDILERNCEEKDYTIWLAHSTDPEDYEDGCILGYKEQFLRLRKSSMCQNGRDYVVT KQPSICLCSLEDFLCDFGYYRPENDSKCVEQPELKGHDLEFCLYGREEHLTTNGYRKIPG DKCQGGVNPVREVKDLKKKCTSNFLSPEKQNSKSNSHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 1 |
| A1JCL | (2~{S})-2-[[6-[3-[8-[2-[(2~{R})-4-[5-[1-[(2-cyanopyridin-3-yl)methyl]-2,2-dimet… | C56 H67 N11 O8 | 1 |
Reshaping the progranulin/sortilin interaction for targeted degradation of extracellular proteins. Gustafsen, C., Vilstrup, J., Kristensen, M. et al. Cell Chem Biol (2026) 33:490. DOI 10.1016/j.chembiol.2026.03.002 · PubMed
Other PDB entries of the same protein (UniProt Q99523 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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