8I0Q: Beta-arrestin1
Structure of beta-arrestin1 in complex with a phosphopeptide corresponding to the human C-X-C chemokine receptor type 4, CXCR4 (Local refine). Determined by electron microscopy at 4.45 Å resolution. Released 17 May 2023.
- Method
- Electron microscopy
- Resolution
- 4.45 Å
- Organisms
- Rattus norvegicus, Mus musculus, Homo sapiens
- Chains
- 8
- Atoms
- 8,842
- Mol. weight
- 196.83 kDa
- Released
- 17 May 2023
Explore 8I0Q in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8I0Q contains 28 α-helices and 105 β-strands across 8 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.
Chain A: 9 helices, 25 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-12 | 6 | 1 |
| β-strand | 19-22 | 4 | 1 |
| β-strand | 26-28 | 3 | 2 |
| β-strand | 29 | 1 | 3 |
| β-strand | 34 | 1 | 3 |
| β-strand | 36-42 | 7 | 1 |
| β-strand | 53-64 | 12 | 4 |
| β-strand | 74-87 | 14 | 4 |
| α-helix | 91-93 | 3 | |
| α-helix | 99-108 | 10 | |
| β-strand | 112-118 | 7 | 1 |
| α-helix | 119-120 | 2 | |
| α-helix | 124-126 | 3 | |
| β-strand | 127-129 | 3 | 4 |
| β-strand | 141-150 | 10 | 4 |
| β-strand | 164-168 | 5 | 4 |
| β-strand | 169-171 | 3 | 2 |
| β-strand | 183-188 | 6 | 5 |
| β-strand | 197-203 | 7 | 5 |
| β-strand | 214-222 | 9 | 5 |
| β-strand | 228-242 | 15 | 6 |
| β-strand | 246-258 | 13 | 6 |
| β-strand | 262 | 1 | 6 |
| β-strand | 266-274 | 9 | 5 |
| α-helix | 279-281 | 3 | |
| β-strand | 288-289 | 2 | 4 |
| β-strand | 300 | 1 | 4 |
| α-helix | 301-303 | 3 | |
| α-helix | 308-310 | 3 | |
| β-strand | 318-329 | 12 | 6 |
| α-helix | 336-338 | 3 | |
| β-strand | 343-349 | 7 | 6 |
| α-helix | 353-356 | 4 | |
| β-strand | 367 | 1 | 7 |
Chain B: 9 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-12 | 6 | 8 |
| β-strand | 18-22 | 5 | 8 |
| β-strand | 26-29 | 4 | 9 |
| β-strand | 34 | 1 | 9 |
| β-strand | 36-43 | 8 | 8 |
| β-strand | 53-64 | 12 | 10 |
| β-strand | 74-87 | 14 | 10 |
| α-helix | 91-93 | 3 | |
| α-helix | 99-108 | 10 | |
| β-strand | 112-118 | 7 | 8 |
| α-helix | 119-120 | 2 | |
| α-helix | 124-126 | 3 | |
| β-strand | 127-129 | 3 | 10 |
| β-strand | 141-150 | 10 | 10 |
| β-strand | 164-168 | 5 | 10 |
| β-strand | 169-172 | 4 | 9 |
| β-strand | 183-188 | 6 | 11 |
| β-strand | 197-203 | 7 | 11 |
| β-strand | 214-222 | 9 | 11 |
| β-strand | 228-242 | 15 | 12 |
| β-strand | 246-258 | 13 | 12 |
| β-strand | 262 | 1 | 12 |
| β-strand | 266-274 | 9 | 11 |
| α-helix | 279-281 | 3 | |
| β-strand | 288-289 | 2 | 10 |
| α-helix | 290-292 | 3 | |
| β-strand | 300 | 1 | 10 |
| α-helix | 301-303 | 3 | |
| α-helix | 308-310 | 3 | |
| β-strand | 318-329 | 12 | 12 |
| α-helix | 336-338 | 3 | |
| β-strand | 343-349 | 7 | 12 |
| β-strand | 367 | 1 | 13 |
Chain H: 2 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-10 | 3 | 14 |
| β-strand | 14-15 | 2 | 15 |
| β-strand | 18 | 1 | 16 |
| β-strand | 23-26 | 4 | 14 |
| β-strand | 35-42 | 8 | 17 |
| β-strand | 49-55 | 7 | 17 |
| β-strand | 60-63 | 4 | 17 |
| α-helix | 65-67 | 3 | |
| β-strand | 68 | 1 | 14 |
| β-strand | 71-76 | 6 | 14 |
| β-strand | 81-86 | 6 | 14 |
| β-strand | 89 | 1 | 16 |
| α-helix | 91-93 | 3 | |
| β-strand | 96-103 | 8 | 17 |
| β-strand | 112-113 | 2 | 17 |
| β-strand | 117-118 | 2 | 17 |
| β-strand | 120-121 | 2 | 15 |
Chain I: 2 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-10 | 3 | 18 |
| β-strand | 14-15 | 2 | 19 |
| β-strand | 18 | 1 | 20 |
| β-strand | 23-26 | 4 | 18 |
| β-strand | 35-42 | 8 | 21 |
| β-strand | 49-54 | 6 | 21 |
| β-strand | 61-63 | 3 | 21 |
| α-helix | 65-67 | 3 | |
| β-strand | 68 | 1 | 18 |
| β-strand | 71-76 | 6 | 18 |
| β-strand | 81-86 | 6 | 18 |
| β-strand | 89 | 1 | 20 |
| α-helix | 91-93 | 3 | |
| β-strand | 96-103 | 8 | 21 |
| β-strand | 112-113 | 2 | 21 |
| β-strand | 117-118 | 2 | 21 |
| β-strand | 120-121 | 2 | 19 |
Chain L: 3 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-8 | 3 | 22 |
| β-strand | 11-12 | 2 | 23 |
| β-strand | 20-25 | 6 | 22 |
| β-strand | 34-39 | 6 | 24 |
| β-strand | 46-50 | 5 | 24 |
| β-strand | 54-55 | 2 | 24 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 22 |
| β-strand | 71-76 | 6 | 22 |
| α-helix | 81-83 | 3 | |
| β-strand | 86-91 | 6 | 24 |
| β-strand | 94 | 1 | 7 |
| α-helix | 97 | 1 | |
| β-strand | 99 | 1 | 24 |
| β-strand | 104-105 | 2 | 23 |
Chain M: 3 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-8 | 4 | 25 |
| β-strand | 11-12 | 2 | 26 |
| β-strand | 20-26 | 7 | 25 |
| β-strand | 34-39 | 6 | 27 |
| β-strand | 46-50 | 5 | 27 |
| β-strand | 54-55 | 2 | 27 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 25 |
| β-strand | 71-76 | 6 | 25 |
| α-helix | 81-83 | 3 | |
| β-strand | 86-91 | 6 | 27 |
| β-strand | 94 | 1 | 13 |
| α-helix | 97 | 1 | |
| β-strand | 99 | 1 | 27 |
| β-strand | 104-105 | 2 | 26 |
Chains U and V: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 345-348 | 4 | 8 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Beta-arrestin-1 | A, B | protein | 418 | Rattus norvegicus | P29066 (AlphaFold model) |
| Fab30 Heavy Chain | H, I | protein | 237 | Mus musculus | |
| Fab30 Light Chain | L, M | protein | 215 | Mus musculus | |
| C-X-C chemokine receptor type 4 | U, V | protein | 17 | Homo sapiens | P61073 (AlphaFold model) |
Sequence of entity 1 (A, B), FASTA
>8I0Q_1 Beta-arrestin-1 (chains A, B)
MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVTLTCA
FRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIP
PNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGP
QPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYAD
ICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNL
ASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEP
PHREVPESETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKDEEDDGTGSPHLNNR
Sequence of entity 2 (H, I), FASTA
>8I0Q_2 Fab30 Heavy Chain (chains H, I)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYGY
TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLVT
VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHHHH
Sequence of entity 3 (L, M), FASTA
>8I0Q_3 Fab30 Light Chain (chains L, M)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 4 (U, V), FASTA
>8I0Q_4 C-X-C chemokine receptor type 4 (chains U, V)
GHSSVSTESESSSFHSS
Primary citation
Structural snapshots uncover a key phosphorylation motif in GPCRs driving beta-arrestin activation. Maharana, J., Sarma, P., Yadav, M.K. et al. Mol Cell (2023) 83:2091-2107.e7. DOI 10.1016/j.molcel.2023.04.025 · PubMed
Other PDB entries of the same protein (UniProt P29066 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4JQI 2.6 Å, Structure of active beta-arrestin1 bound to a G protein-coupled receptor phosphopeptide
- 8HST 2.66 Å, The structure of rat beta-arrestin1
- 9KYU 2.72 Å, Structure of beta-arrestin1 in complex with mouse C5aR1pp
- 6KL7 2.79 Å, Beta-arrestin 1 mutant S13D/T275D
- 8HSV 3.0 Å, The structure of rat beta-arrestin1 in complex with a rat Mdm2 peptide
- 8I0N 3.26 Å, Structure of beta-arrestin1 in complex with a phosphopeptide corresponding to the human…
- 9BT8 3.34 Å, Structure of Src in complex with beta-arrestin 1 revealing SH3 binding sites
- 9CX9 3.34 Å, Structure of SH3 domain of Src in complex with beta-arrestin 1
- 8J8Z 3.4 Å, Structure of beta-arrestin1 in complex with D6Rpp
- 8GO8 3.41 Å, Structure of beta-arrestin1 in complex with a phosphopeptide corresponding to the human…
- 9CX3 3.47 Å, Structure of SH3 domain of Src in complex with beta-arrestin 1
- 9DNM 3.47 Å, Structure of rat beta-arrestin 1 bound to allosteric inhibitor
Browse structure collections
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