ACKR3 phosphorylated by GRK5 in complex with arrestin2 and Fab7. Determined by electron microscopy at 3.4 Å resolution. Released 2 Apr 2025.
Explore 9E82 in 3D Show helices and sheets RCSB PDB PDBe
9E82 contains 32 α-helices and 78 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-12 | 6 | 1 |
| β-strand | 18-21 | 4 | 1 |
| β-strand | 26-28 | 3 | 2 |
| β-strand | 29 | 1 | 3 |
| β-strand | 34 | 1 | 3 |
| α-helix | 35-36 | 2 | |
| β-strand | 38-43 | 6 | 1 |
| β-strand | 53-62 | 10 | 4 |
| β-strand | 78-87 | 10 | 4 |
| α-helix | 96-98 | 3 | |
| α-helix | 99-108 | 10 | |
| β-strand | 112-116 | 5 | 1 |
| α-helix | 119-120 | 2 | |
| β-strand | 127-129 | 3 | 5 |
| α-helix | 130-132 | 3 | |
| α-helix | 138-139 | 2 | |
| β-strand | 141-150 | 10 | 4 |
| β-strand | 163-168 | 6 | 4 |
| β-strand | 169-171 | 3 | 2 |
| α-helix | 173-175 | 3 | |
| β-strand | 184-188 | 5 | 6 |
| α-helix | 196 | 1 | |
| β-strand | 197-201 | 5 | 6 |
| β-strand | 203 | 1 | 6 |
| β-strand | 208-209 | 2 | 7 |
| β-strand | 214-222 | 9 | 6 |
| β-strand | 228-230 | 3 | 8 |
| β-strand | 231-234 | 4 | 9 |
| β-strand | 237-242 | 6 | 10 |
| β-strand | 249-251 | 3 | 10 |
| β-strand | 255-258 | 4 | 9 |
| β-strand | 266-274 | 9 | 6 |
| α-helix | 278-280 | 3 | |
| β-strand | 288-290 | 3 | 5 |
| β-strand | 300 | 1 | 5 |
| α-helix | 301-304 | 4 | |
| β-strand | 316-327 | 12 | 10 |
| β-strand | 328-329 | 2 | 8 |
| β-strand | 343-349 | 7 | 10 |
| β-strand | 351-352 | 2 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 11 |
| β-strand | 21-28 | 8 | 11 |
| α-helix | 32-34 | 3 | |
| β-strand | 35-42 | 8 | 12 |
| β-strand | 50-55 | 6 | 12 |
| β-strand | 60-63 | 4 | 12 |
| α-helix | 65-67 | 3 | |
| β-strand | 71 | 1 | 11 |
| β-strand | 74-76 | 3 | 11 |
| β-strand | 81-86 | 6 | 11 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-103 | 9 | 12 |
| β-strand | 105 | 1 | 13 |
| β-strand | 111 | 1 | 13 |
| β-strand | 121-122 | 2 | 12 |
| β-strand | 127-128 | 2 | 12 |
| β-strand | 136 | 1 | 14 |
| β-strand | 139-143 | 5 | 15 |
| β-strand | 155-164 | 10 | 15 |
| β-strand | 165 | 1 | 14 |
| β-strand | 170-173 | 4 | 16 |
| β-strand | 183-184 | 2 | 15 |
| α-helix | 185-187 | 3 | |
| β-strand | 195-203 | 9 | 15 |
| α-helix | 205-207 | 3 | |
| β-strand | 213-219 | 7 | 16 |
| β-strand | 224-230 | 7 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 17 |
| β-strand | 8 | 1 | 18 |
| β-strand | 11-13 | 3 | 19 |
| β-strand | 20-25 | 6 | 18 |
| β-strand | 26 | 1 | 17 |
| β-strand | 34-36 | 3 | 20 |
| β-strand | 49-50 | 2 | 20 |
| β-strand | 54-55 | 2 | 20 |
| α-helix | 56 | 1 | |
| β-strand | 63-66 | 4 | 18 |
| β-strand | 71-76 | 6 | 18 |
| β-strand | 89-91 | 3 | 20 |
| β-strand | 98-99 | 2 | 20 |
| β-strand | 104-106 | 3 | 19 |
| β-strand | 112 | 1 | 21 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-119 | 5 | 22 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-128 | 6 | |
| β-strand | 130-140 | 11 | 22 |
| β-strand | 141 | 1 | 21 |
| β-strand | 145-150 | 6 | 23 |
| β-strand | 160-161 | 2 | 22 |
| β-strand | 164 | 1 | 22 |
| α-helix | 165-168 | 4 | |
| β-strand | 174-183 | 10 | 22 |
| α-helix | 184-187 | 4 | |
| β-strand | 192-199 | 8 | 23 |
| β-strand | 206-211 | 6 | 23 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 40-69 | 30 | |
| α-helix | 81-105 | 25 | |
| α-helix | 114-145 | 32 | |
| α-helix | 158-181 | 24 | |
| β-strand | 183-187 | 5 | 24 |
| β-strand | 194-198 | 5 | 24 |
| α-helix | 202-204 | 3 | |
| α-helix | 208-214 | 7 | |
| α-helix | 215-222 | 8 | |
| α-helix | 223-238 | 16 | |
| α-helix | 253-279 | 27 | |
| α-helix | 287-310 | 24 | |
| α-helix | 311-313 | 3 | |
| β-strand | 339-342 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-arrestin-1 | A | protein | 418 | Bos taurus | P17870 (AlphaFold model) |
| SDF-1-beta(3-72) | B | protein | 69 | Homo sapiens | P48061 (AlphaFold model) |
| Fab7 heavy chain | H | protein | 240 | synthetic construct | |
| Fab7 light chain | L | protein | 215 | synthetic construct | |
| Atypical chemokine receptor 3 | R | protein | 393 | Homo sapiens | P25106 (AlphaFold model) |
>9E82_1 Beta-arrestin-1 (chains A) MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVEPVDGVVLVDPEYLKERRVYVTLTCA FRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIP PNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGP QPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYAD ICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNL ASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEP PHREVPEHETPVDTNLIELDTNDDDAAAEDFARQRLKGMKDDKEEEEDGTGSPRLNDR
>9E82_2 SDF-1-beta(3-72) (chains B) LRHQSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQ EYLEKALNK
>9E82_3 Fab7 heavy chain (chains H) EISEVQLVESGGGLVQPGGSLRLSCAASGFNVSSSYIHWVRQAPGKGLEWVASISSYYGY TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARKSMYHRGWGWLSWVYGAMD YWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTS GVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT
>9E82_4 Fab7 light chain (chains L) SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP SRFSGSRSGTDFTLTISSLQPEDFATYYCQQSYYYPITFGQGTKVEIKRTVAAPSVFIFP PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>9E82_5 Atypical chemokine receptor 3 (chains R) GAPDLHLFDYSEPGNFSDISWPCNSSDCIVVDTVMCPNMPNKSVLLYTLSFIYIFIFVIG MIANSVVVWVNIQAKTTGYDTHCYILNLAIADLWVVLTIPVWVVSLVQHNQWPMGELTCK VTHLIFSINLFGSIFFLTCMSVDRYLSITYFTNTPSSRKKMVRRVVCILVWLLAFCVSLP DTYYLKTVTSASNNETYCRSFYPEHSIKEWLIGMELVSVVLGFAVPFSIIAVFYFLLARA ISASSDQEKHSSRKIIFSYVVVFLVCWLPYHVAVLLDIFSILHYIPFTCRLEHALFTALH VTQCLSLVHCCVNPVLYSFINRNYRYELMKAFIFKYSAKTGLTKLIDASRVSETEYSALE QSTKGRPLEVLFQGPHHHHHHHHHHDYKDDDDK
| ID | Name | Formula | Copies |
|---|---|---|---|
| CLR | Cholesterol | C27 H46 O | 1 |
Effect of phosphorylation barcodes on arrestin binding to a chemokine receptor. Chen, Q., Schafer, C.T., Mukherjee, S. et al. Nature (2025) 643:280-287. DOI 10.1038/s41586-025-09024-9 · PubMed
Other PDB entries of the same protein (UniProt P17870 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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