8I10: Beta-arrestin2
Structure of beta-arrestin2 in complex with a phosphopeptide corresponding to the human Vasopressin V2 receptor, V2R (Local refine). Determined by electron microscopy at 3.96 Å resolution. Released 17 May 2023.
- Method
- Electron microscopy
- Resolution
- 3.96 Å
- Organisms
- Bos taurus, Mus musculus, Homo sapiens
- Chains
- 12
- Atoms
- 13,196
- Mol. weight
- 299.15 kDa
- Released
- 17 May 2023
Explore 8I10 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8I10 contains 43 α-helices and 152 β-strands across 12 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: 11 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-13 | 4 | 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 | 40-44 | 5 | 1 |
| β-strand | 53-61 | 9 | 4 |
| β-strand | 79-88 | 10 | 4 |
| α-helix | 90-91 | 2 | |
| α-helix | 100-109 | 10 | |
| β-strand | 113-116 | 4 | 1 |
| β-strand | 128-130 | 3 | 5 |
| α-helix | 131-133 | 3 | |
| β-strand | 144-152 | 9 | 4 |
| α-helix | 158-159 | 2 | |
| β-strand | 164-169 | 6 | 4 |
| β-strand | 170-172 | 3 | 2 |
| α-helix | 181-183 | 3 | |
| β-strand | 184-190 | 7 | 6 |
| β-strand | 197-204 | 8 | 6 |
| β-strand | 208-209 | 2 | 7 |
| α-helix | 213-214 | 2 | |
| β-strand | 215-224 | 10 | 6 |
| β-strand | 229-240 | 12 | 8 |
| β-strand | 243 | 1 | 9 |
| β-strand | 247 | 1 | 9 |
| β-strand | 250-259 | 10 | 8 |
| β-strand | 263 | 1 | 8 |
| β-strand | 267-275 | 9 | 6 |
| α-helix | 280-282 | 3 | |
| α-helix | 288 | 1 | |
| β-strand | 289-291 | 3 | 5 |
| α-helix | 292-293 | 2 | |
| α-helix | 300 | 1 | |
| β-strand | 301 | 1 | 5 |
| α-helix | 302-305 | 4 | |
| β-strand | 320-330 | 11 | 8 |
| β-strand | 336-342 | 7 | 8 |
| β-strand | 343-344 | 2 | 7 |
Chain B: 9 helices, 27 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-13 | 4 | 10 |
| β-strand | 19-23 | 5 | 10 |
| β-strand | 27-29 | 3 | 11 |
| β-strand | 30 | 1 | 12 |
| β-strand | 35 | 1 | 12 |
| β-strand | 40-44 | 5 | 10 |
| β-strand | 53-63 | 11 | 13 |
| β-strand | 78-82 | 5 | 13 |
| β-strand | 85-88 | 4 | 13 |
| α-helix | 100-109 | 10 | |
| α-helix | 110-112 | 3 | |
| β-strand | 113-116 | 4 | 10 |
| β-strand | 128-130 | 3 | 13 |
| α-helix | 131-133 | 3 | |
| β-strand | 142-152 | 11 | 13 |
| α-helix | 161-163 | 3 | |
| β-strand | 164-167 | 4 | 13 |
| β-strand | 170-172 | 3 | 11 |
| α-helix | 181-183 | 3 | |
| β-strand | 184-190 | 7 | 14 |
| β-strand | 197-204 | 8 | 14 |
| β-strand | 208-209 | 2 | 15 |
| α-helix | 213-214 | 2 | |
| β-strand | 215-224 | 10 | 14 |
| β-strand | 229-240 | 12 | 16 |
| β-strand | 250-259 | 10 | 16 |
| β-strand | 263 | 1 | 16 |
| β-strand | 267-275 | 9 | 14 |
| α-helix | 280-282 | 3 | |
| β-strand | 289-291 | 3 | 13 |
| α-helix | 300 | 1 | |
| β-strand | 301 | 1 | 13 |
| α-helix | 302-303 | 2 | |
| β-strand | 320-330 | 11 | 16 |
| β-strand | 336-342 | 7 | 16 |
| β-strand | 343-344 | 2 | 15 |
Chain C: 12 helices, 26 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 10-13 | 4 | 17 |
| β-strand | 19-23 | 5 | 17 |
| β-strand | 27-29 | 3 | 18 |
| β-strand | 30 | 1 | 19 |
| β-strand | 35 | 1 | 19 |
| β-strand | 40-44 | 5 | 17 |
| β-strand | 53-62 | 10 | 20 |
| β-strand | 78-88 | 11 | 20 |
| α-helix | 90-91 | 2 | |
| α-helix | 100-109 | 10 | |
| β-strand | 113-116 | 4 | 17 |
| β-strand | 128-130 | 3 | 21 |
| α-helix | 131-133 | 3 | |
| β-strand | 144-152 | 9 | 20 |
| α-helix | 158-159 | 2 | |
| β-strand | 164-169 | 6 | 20 |
| β-strand | 170-172 | 3 | 18 |
| α-helix | 181-183 | 3 | |
| β-strand | 184-190 | 7 | 22 |
| β-strand | 197-203 | 7 | 22 |
| β-strand | 208-209 | 2 | 23 |
| α-helix | 213-214 | 2 | |
| β-strand | 215-224 | 10 | 22 |
| β-strand | 229-242 | 14 | 24 |
| β-strand | 248-259 | 12 | 24 |
| β-strand | 263 | 1 | 24 |
| β-strand | 267-275 | 9 | 22 |
| α-helix | 280-282 | 3 | |
| α-helix | 288 | 1 | |
| β-strand | 289-291 | 3 | 21 |
| α-helix | 292-293 | 2 | |
| α-helix | 300 | 1 | |
| β-strand | 301 | 1 | 21 |
| α-helix | 302-305 | 4 | |
| β-strand | 318-330 | 13 | 24 |
| β-strand | 336-342 | 7 | 24 |
| β-strand | 343-344 | 2 | 23 |
| α-helix | 346-349 | 4 | |
Chain D: 2 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-10 | 5 | 25 |
| β-strand | 13-15 | 3 | 26 |
| β-strand | 21-28 | 8 | 25 |
| β-strand | 35-42 | 8 | 26 |
| α-helix | 47-48 | 2 | |
| β-strand | 49-54 | 6 | 26 |
| β-strand | 61-63 | 3 | 26 |
| β-strand | 71-76 | 6 | 25 |
| β-strand | 81-86 | 6 | 25 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-103 | 9 | 26 |
| β-strand | 112-113 | 2 | 26 |
| β-strand | 117-121 | 5 | 26 |
Chain E: 2 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-8 | 4 | 27 |
| β-strand | 11-12 | 2 | 28 |
| β-strand | 20-26 | 7 | 27 |
| β-strand | 34-39 | 6 | 28 |
| β-strand | 46-50 | 5 | 28 |
| β-strand | 54-55 | 2 | 28 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 27 |
| β-strand | 71-76 | 6 | 27 |
| β-strand | 86-91 | 6 | 28 |
| α-helix | 97 | 1 | |
| β-strand | 98-99 | 2 | 28 |
| β-strand | 103-105 | 3 | 28 |
Chains G, U and V: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 361-362 | 2 | 1 |
Chain H: 2 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-10 | 5 | 29 |
| β-strand | 13-14 | 2 | 30 |
| β-strand | 21-28 | 8 | 29 |
| β-strand | 35-42 | 8 | 30 |
| α-helix | 47-48 | 2 | |
| β-strand | 49-54 | 6 | 30 |
| β-strand | 61-63 | 3 | 30 |
| β-strand | 71-76 | 6 | 29 |
| β-strand | 81-86 | 6 | 29 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-103 | 9 | 30 |
| β-strand | 112-113 | 2 | 30 |
| β-strand | 117-120 | 4 | 30 |
Chain L: 2 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-8 | 4 | 31 |
| β-strand | 11-14 | 4 | 32 |
| β-strand | 20-26 | 7 | 31 |
| β-strand | 34-39 | 6 | 32 |
| β-strand | 45-50 | 6 | 32 |
| β-strand | 54-55 | 2 | 32 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 31 |
| β-strand | 71-76 | 6 | 31 |
| β-strand | 86-91 | 6 | 32 |
| α-helix | 97 | 1 | |
| β-strand | 98-99 | 2 | 32 |
| β-strand | 103-107 | 5 | 32 |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Beta-arrestin-2 | A, B, C | protein | 420 | Bos taurus | P32120 (AlphaFold model) |
| Fab30 Heavy Chain | D, H, M | protein | 237 | Mus musculus | |
| Fab30 Light Chain | E, L, N | protein | 215 | Mus musculus | |
| Vasopressin V2 receptor | G, U, V | protein | 29 | Homo sapiens | P30518 (AlphaFold model) |
Sequence of entity 1 (A, B, C), FASTA
>8I10_1 Beta-arrestin-2 (chains A, B, C)
MGEKPGTRVFKKSSPNGKLTVYLGKRDFVDHLDKVDPVDGVVLVDPDYLKDRKVFVTLTV
AFRYGREDCDVLGLSFRKDLFIANYQAFPPTPNPPRPPTRLQERLLRKLGQHAHPFFFTI
PQNLPSSVTLQPGPEDTGKALGVDFEIRAFVAKSLEEKSHKRNSVRLVIRKVQFAPEKPG
PQPSAETTRHFLMSDRSLHLEASLDKELYYHGEPLNVNVHVTNNSTKTVKKIKVSVRQYA
DIVLFSTAQYKVPVAQVEQDDQVSPSSTFSKVYTITPFLANNREKRGLALDGKLKHEDTN
LASSTIVKEGANKEVLGILVSYRVKVKLVVSRGGDVSVELPFVLMHPKPHDHIALPRPQS
AATHPPTLLPSAVPETDAPVDTNLIEFETNYATDDDIVFEDFARLRLKGLKDEDYDDQFC
Sequence of entity 2 (D, H, M), FASTA
>8I10_2 Fab30 Heavy Chain (chains D, H, M)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGLEWVASISSYYGY
TYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYSGLDYWGQGTLVT
VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHHHHHHHH
Sequence of entity 3 (E, L, N), FASTA
>8I10_3 Fab30 Light Chain (chains E, L, N)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
Sequence of entity 4 (G, U, V), FASTA
>8I10_4 Vasopressin V2 receptor (chains G, U, V)
ARGRTPPSLGPQDESCTTASSSLAKDTSS
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 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…
- 8J8V 3.22 Å, Structure of beta-arrestin2 in complex with D6Rpp (Local Refine)
- 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…
- 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…
Browse structure collections
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