Structure of Duffy Antigen Receptor for Chemokines (DARC)/ACKR1 in complex with the chemokine, CCL7 (Composite map). Determined by electron microscopy at 3.65 Å resolution. Released 31 Jul 2024.
Explore 8JPS in 3D Show helices and sheets RCSB PDB PDBe
8JPS contains 38 α-helices and 15 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 |
|---|---|---|---|
| α-helix | 49-50 | 2 | |
| β-strand | 51-52 | 2 | 4 |
| α-helix | 53 | 1 | |
| α-helix | 59-61 | 3 | |
| α-helix | 63-81 | 19 | |
| α-helix | 86-88 | 3 | |
| α-helix | 96-112 | 17 | |
| α-helix | 113-116 | 4 | |
| α-helix | 126-152 | 27 | |
| α-helix | 154-157 | 4 | |
| α-helix | 163-180 | 18 | |
| α-helix | 182-186 | 5 | |
| β-strand | 188-192 | 5 | 5 |
| β-strand | 194-197 | 4 | 5 |
| α-helix | 204-215 | 12 | |
| α-helix | 216-220 | 5 | |
| α-helix | 221-226 | 6 | |
| α-helix | 245-248 | 4 | |
| α-helix | 250-252 | 3 | |
| α-helix | 254-267 | 14 | |
| α-helix | 276-294 | 19 | |
| α-helix | 296-311 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 49-50 | 2 | |
| β-strand | 51 | 1 | 1 |
| α-helix | 59-61 | 3 | |
| α-helix | 63-81 | 19 | |
| α-helix | 86-88 | 3 | |
| α-helix | 96-112 | 17 | |
| α-helix | 113-115 | 3 | |
| α-helix | 126-157 | 32 | |
| α-helix | 163-180 | 18 | |
| α-helix | 182-186 | 5 | |
| β-strand | 188-190 | 3 | 2 |
| β-strand | 195-197 | 3 | 2 |
| α-helix | 201-203 | 3 | |
| α-helix | 204-215 | 12 | |
| α-helix | 216-220 | 5 | |
| α-helix | 221-225 | 5 | |
| α-helix | 245-247 | 3 | |
| α-helix | 248-267 | 20 | |
| α-helix | 276-294 | 19 | |
| α-helix | 296-310 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-11 | 2 | 4 |
| β-strand | 16 | 1 | 6 |
| β-strand | 25-30 | 6 | 6 |
| β-strand | 41-45 | 5 | 6 |
| β-strand | 50-53 | 4 | 6 |
| α-helix | 58-66 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11 | 1 | 1 |
| β-strand | 25-29 | 5 | 3 |
| β-strand | 41-45 | 5 | 3 |
| β-strand | 50-53 | 4 | 3 |
| α-helix | 58-66 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Atypical chemokine receptor 1 | A, B | protein | 267 | Homo sapiens | Q16570 (AlphaFold model) |
| C-C motif chemokine 7 | C, D | protein | 63 | Homo sapiens | P80098 (AlphaFold model) |
>8JPS_1 Atypical chemokine receptor 1 (chains A, B) EAAAPCHSCNLLDDSALPFFILTSVLGILASSTVLFMLFRPLFRWQLCPGWPVLAQLAVG SALFSIVVPVLAPGLGSTRSSALCSLGYCVWYGSAFAQALLLGCHASLGHRLGAGQVPGL TLGLTVGIWGVAALLTLPVTLASGASGGLCTLIYSTELKALQATHTVACLAIFVLLPLGL FGAKGLKKALGMGPGPWMNILWAWFIFWWPHGVVLGLDFLVRSKLLLLSTCLAQQALDLL LNLAEALAILHCVATPLLLALFCHQAT
>8JPS_2 C-C motif chemokine 7 (chains C, D) STTCCYRFINKKIPKQRLESYRRTTSSHCPREAVIFKTKLDKEICADPTQKWVQDFMKHL DKK
Molecular mechanism of distinct chemokine engagement and functional divergence of the human Duffy antigen receptor. Saha, S., Khanppnavar, B., Maharana, J. et al. Cell (2024) 187:4751-4769.e25. DOI 10.1016/j.cell.2024.07.005 · PubMed
Other PDB entries of the same protein (UniProt Q16570 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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