Structure of arrestin2 in complex with 6P CCR5 phosphopeptide and Fab30. Determined by X-ray diffraction at 3.5 Å resolution. Released 7 Jun 2023.
Explore 8AS3 in 3D Show helices and sheets RCSB PDB PDBe
8AS3 contains 22 α-helices and 73 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 | 18-22 | 5 | 1 |
| β-strand | 26-28 | 3 | 2 |
| β-strand | 29 | 1 | 3 |
| β-strand | 34 | 1 | 3 |
| β-strand | 37-43 | 7 | 1 |
| β-strand | 53-63 | 11 | 4 |
| β-strand | 75-87 | 13 | 4 |
| α-helix | 96-98 | 3 | |
| α-helix | 99-108 | 10 | |
| β-strand | 112-117 | 6 | 1 |
| α-helix | 123-125 | 3 | |
| β-strand | 127-129 | 3 | 4 |
| α-helix | 130-132 | 3 | |
| α-helix | 138-140 | 3 | |
| β-strand | 141-150 | 10 | 4 |
| α-helix | 157-159 | 3 | |
| α-helix | 160-162 | 3 | |
| β-strand | 163-168 | 6 | 4 |
| β-strand | 169-171 | 3 | 2 |
| α-helix | 180-182 | 3 | |
| β-strand | 183-189 | 7 | 5 |
| β-strand | 196-203 | 8 | 5 |
| β-strand | 207-208 | 2 | 6 |
| β-strand | 214-222 | 9 | 5 |
| β-strand | 227-242 | 16 | 7 |
| β-strand | 247-258 | 12 | 7 |
| β-strand | 262 | 1 | 7 |
| β-strand | 266-274 | 9 | 5 |
| α-helix | 279-281 | 3 | |
| β-strand | 288-290 | 3 | 4 |
| β-strand | 300 | 1 | 4 |
| α-helix | 301-304 | 4 | |
| β-strand | 316-330 | 15 | 7 |
| α-helix | 333-335 | 3 | |
| β-strand | 343-349 | 7 | 7 |
| β-strand | 350-351 | 2 | 6 |
| α-helix | 353-356 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 341-344 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-10 | 5 | 8 |
| β-strand | 14-15 | 2 | 9 |
| β-strand | 20-28 | 9 | 8 |
| β-strand | 35-42 | 8 | 10 |
| β-strand | 50-55 | 6 | 10 |
| β-strand | 60-63 | 4 | 10 |
| β-strand | 71-76 | 6 | 8 |
| β-strand | 81-87 | 7 | 8 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-103 | 9 | 10 |
| β-strand | 112-113 | 2 | 10 |
| β-strand | 117-119 | 3 | 10 |
| β-strand | 120-121 | 2 | 9 |
| β-strand | 130-133 | 4 | 11 |
| β-strand | 142 | 1 | 11 |
| β-strand | 145-155 | 11 | 11 |
| β-strand | 161-164 | 4 | 12 |
| α-helix | 165-167 | 3 | |
| β-strand | 169 | 1 | 12 |
| β-strand | 174-175 | 2 | 11 |
| α-helix | 176-178 | 3 | |
| β-strand | 179-180 | 2 | 11 |
| β-strand | 186-195 | 10 | 11 |
| β-strand | 199 | 1 | 13 |
| β-strand | 202 | 1 | 13 |
| β-strand | 205 | 1 | 14 |
| β-strand | 206-209 | 4 | 12 |
| β-strand | 217 | 1 | 12 |
| β-strand | 220 | 1 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 15 |
| β-strand | 13 | 1 | 16 |
| β-strand | 20-26 | 7 | 15 |
| β-strand | 34-39 | 6 | 17 |
| β-strand | 46-50 | 5 | 17 |
| β-strand | 54-55 | 2 | 17 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 15 |
| β-strand | 71-76 | 6 | 15 |
| β-strand | 86-91 | 6 | 17 |
| α-helix | 97 | 1 | |
| β-strand | 98-99 | 2 | 17 |
| β-strand | 103-104 | 2 | 17 |
| β-strand | 106 | 1 | 16 |
| α-helix | 112-114 | 3 | |
| β-strand | 117-119 | 3 | 18 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-128 | 6 | |
| β-strand | 130-140 | 11 | 18 |
| β-strand | 148-151 | 4 | 19 |
| β-strand | 154-155 | 2 | 19 |
| β-strand | 160-164 | 5 | 18 |
| α-helix | 165-168 | 4 | |
| β-strand | 174-183 | 10 | 18 |
| α-helix | 184-188 | 5 | |
| β-strand | 194-197 | 4 | 19 |
| β-strand | 206-209 | 4 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-arrestin-1 | A | protein | 359 | Homo sapiens | P49407 (AlphaFold model) |
| C-C chemokine receptor type 5 | B | protein | 21 | Homo sapiens | P51681 (AlphaFold model) |
| Fab30 heavy chain | H | protein | 233 | Phage display vector pTDisp | |
| Fab30 light chain | L | protein | 220 | Phage display vector pTDisp |
>8AS3_1 Beta-arrestin-1 (chains A) MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCA FRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIP PNLPCSVTLQPGPEDTGKACGVDYEVKAFLAENLEEKIHKRNSVRLVIRKVQYAPERPGP QPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYAD IVLFNTAQYKVPVAMEEADDTVAPSSTFSKVYTLTPFLANNREKRGLALDGKLKHEDTNL ASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEE
>8AS3_2 C-C chemokine receptor type 5 (chains B) APERASSVYTRSTGEQEISVG
>8AS3_3 Fab30 heavy chain (chains H) VQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYGYTYYA DSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLVTVSSA STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHHHH
>8AS3_4 Fab30 light chain (chains L) SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKRTVAAPSVFIFP PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGECEISEV
A key GPCR phosphorylation motif discovered in arrestin2⋅CCR5 phosphopeptide complexes. Isaikina, P., Petrovic, I., Jakob, R.P. et al. Mol Cell (2023) 83:2108. DOI 10.1016/j.molcel.2023.05.002 · PubMed
Other PDB entries of the same protein (UniProt P49407 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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