8J8V: Beta-arrestin2
Structure of beta-arrestin2 in complex with D6Rpp (Local Refine). Determined by electron microscopy at 3.22 Å resolution. Released 27 Dec 2023.
- Method
- Electron microscopy
- Resolution
- 3.22 Å
- Organisms
- Bos taurus, Mus musculus, Homo sapiens
- Chains
- 8
- Atoms
- 9,437
- Mol. weight
- 197.04 kDa
- Released
- 27 Dec 2023
Explore 8J8V in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8J8V contains 23 α-helices and 104 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: 8 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-13 | 7 | 1 |
| β-strand | 19-23 | 5 | 1 |
| β-strand | 27-29 | 3 | 2 |
| β-strand | 30 | 1 | 3 |
| β-strand | 35 | 1 | 3 |
| β-strand | 38-44 | 7 | 1 |
| β-strand | 53-63 | 11 | 4 |
| β-strand | 73 | 1 | 5 |
| β-strand | 76 | 1 | 6 |
| β-strand | 78-88 | 11 | 4 |
| α-helix | 100-109 | 10 | |
| α-helix | 110-112 | 3 | |
| β-strand | 113-118 | 6 | 1 |
| β-strand | 128-130 | 3 | 4 |
| α-helix | 131-133 | 3 | |
| β-strand | 142-152 | 11 | 4 |
| α-helix | 158-159 | 2 | |
| β-strand | 165-169 | 5 | 4 |
| β-strand | 170-172 | 3 | 2 |
| α-helix | 181-183 | 3 | |
| β-strand | 184-190 | 7 | 7 |
| β-strand | 197-204 | 8 | 7 |
| β-strand | 208-209 | 2 | 8 |
| β-strand | 215-223 | 9 | 7 |
| β-strand | 229-243 | 15 | 9 |
| β-strand | 247-259 | 13 | 9 |
| β-strand | 263 | 1 | 9 |
| β-strand | 267-275 | 9 | 7 |
| β-strand | 289-291 | 3 | 4 |
| β-strand | 301 | 1 | 4 |
| α-helix | 302-304 | 3 | |
| β-strand | 317-330 | 14 | 9 |
| β-strand | 336-342 | 7 | 9 |
| β-strand | 343-344 | 2 | 8 |
| α-helix | 346-349 | 4 | |
| α-helix | 394-407 | 14 | |
Chain B: 1 helix, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-10 | 5 | 10 |
| β-strand | 13-14 | 2 | 11 |
| β-strand | 20-28 | 9 | 10 |
| β-strand | 35-42 | 8 | 11 |
| β-strand | 48-55 | 8 | 11 |
| β-strand | 60-63 | 4 | 11 |
| β-strand | 68 | 1 | 10 |
| β-strand | 71-76 | 6 | 10 |
| β-strand | 81-87 | 7 | 10 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-103 | 9 | 11 |
| β-strand | 112-113 | 2 | 11 |
| β-strand | 117-120 | 4 | 11 |
Chains C and E: 3 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-8 | 4 | 12 |
| β-strand | 11-13 | 3 | 13 |
| β-strand | 20-26 | 7 | 12 |
| β-strand | 34-39 | 6 | 13 |
| α-helix | 44-45 | 2 | |
| β-strand | 46-50 | 5 | 13 |
| β-strand | 54-55 | 2 | 13 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 12 |
| β-strand | 71-76 | 6 | 12 |
| β-strand | 86-91 | 6 | 13 |
| α-helix | 97 | 1 | |
| β-strand | 98-99 | 2 | 13 |
| β-strand | 103-106 | 4 | 13 |
Chain D: 1 helix, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-10 | 5 | 14 |
| β-strand | 13-15 | 3 | 15 |
| β-strand | 20-28 | 9 | 14 |
| β-strand | 35-42 | 8 | 15 |
| β-strand | 48-55 | 8 | 15 |
| β-strand | 60-63 | 4 | 15 |
| β-strand | 68 | 1 | 14 |
| β-strand | 71-76 | 6 | 14 |
| β-strand | 81-87 | 7 | 14 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-103 | 9 | 15 |
| β-strand | 112-113 | 2 | 15 |
| β-strand | 117-121 | 5 | 15 |
Chain F: 7 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-13 | 7 | 18 |
| β-strand | 20-23 | 4 | 18 |
| β-strand | 27-29 | 3 | 19 |
| β-strand | 30 | 1 | 20 |
| β-strand | 35 | 1 | 20 |
| β-strand | 38-43 | 6 | 18 |
| β-strand | 53-63 | 11 | 21 |
| β-strand | 73 | 1 | 6 |
| β-strand | 76 | 1 | 5 |
| β-strand | 78-88 | 11 | 21 |
| α-helix | 90-92 | 3 | |
| α-helix | 100-109 | 10 | |
| β-strand | 113-118 | 6 | 18 |
| β-strand | 128-130 | 3 | 21 |
| α-helix | 131-133 | 3 | |
| β-strand | 142-152 | 11 | 21 |
| α-helix | 158-159 | 2 | |
| β-strand | 165-169 | 5 | 21 |
| β-strand | 170-172 | 3 | 19 |
| β-strand | 184-190 | 7 | 22 |
| β-strand | 197-204 | 8 | 22 |
| β-strand | 208-209 | 2 | 23 |
| β-strand | 215-223 | 9 | 22 |
| β-strand | 229-243 | 15 | 24 |
| β-strand | 247-259 | 13 | 24 |
| β-strand | 263 | 1 | 24 |
| β-strand | 267-275 | 9 | 22 |
| β-strand | 289-291 | 3 | 21 |
| β-strand | 301 | 1 | 21 |
| α-helix | 302-304 | 3 | |
| β-strand | 317-330 | 14 | 24 |
| β-strand | 336-342 | 7 | 24 |
| β-strand | 343-344 | 2 | 23 |
| α-helix | 346-349 | 4 | |
| α-helix | 394-407 | 14 | |
Chains G and H: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 349-353 | 5 | 1 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Beta-arrestin-2 | A, F | protein | 420 | Bos taurus | P32120 (AlphaFold model) |
| Fab30 Heavy Chain | B, D | protein | 237 | Mus musculus | |
| Fab30 Light Chain | C, E | protein | 215 | Mus musculus | |
| Atypical chemokine receptor 2 | G, H | protein | 18 | Homo sapiens | O00590 (AlphaFold model) |
Sequence of entity 1 (A, F), FASTA
>8J8V_1 Beta-arrestin-2 (chains A, F)
MGEKPGTRVFKKSSPNGKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTV
AFRYGREDCDVLGLSFRKDLFIANYQAFPPTPNPPRPPTRLQERLLRKLGQHAHPFFFTI
PQNLPSSVTLQPGPEDTGKALGVDFEIRAFVAKSLEEKSHKRNSVRLVIRKVQFAPEKPG
PQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYA
DIVLFSTAQYKVPVAQVEQDDQVSPSSTFSKVYTITPFLANNREKRGLALDGKLKHEDTN
LASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIALPRPQS
AATHPPTLLPSAVPETDAPVDTNLIEFETNYATDDDIVFEDFARLRLKGLKDEDYDDQFC
Sequence of entity 2 (B, D), FASTA
>8J8V_2 Fab30 Heavy Chain (chains B, D)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYGY
TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLVT
VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHHHH
Sequence of entity 3 (C, E), FASTA
>8J8V_3 Fab30 Light Chain (chains C, E)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 4 (G, H), FASTA
>8J8V_4 Atypical chemokine receptor 2 (chains G, H)
GTAQASLSSCSESSILTA
Primary citation
Molecular insights into atypical modes of beta-arrestin interaction with seven transmembrane receptors. Maharana, J., Sano, F.K., Sarma, P. et al. Science (2024) 383:101-108. DOI 10.1126/science.adj3347 · PubMed
Other PDB entries of the same protein (UniProt P32120 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5TV1 2.4 Å, active arrestin-3 with inositol hexakisphosphate
- 9KY2 2.78 Å, Structure of beta-arrestin2 in complex with mouse C5aR1pp
- 8J8R 2.9 Å, Structure of beta-arrestin2 in complex with M2Rpp
- 3P2D 3.0 Å, Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding…
- 8VJ9 3.3 Å, CryoEM structure of human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 variant…
- 8GO9 3.35 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…
- 8TIL 3.8 Å, Human ACKR3 phosphorylated by GRK5 in complex with Arrestin3 reconstructed without…
- 8I10 3.96 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…
- 8TIN 4.0 Å, Human ACKR3 phosphorylated by GRK2 in complex with Arrestin3 reconstructed without…
- 8GOC 4.18 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…
- 8I0Z 4.33 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…
- 8GOO 4.4 Å, Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human…
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