The structure of rat beta-arrestin1 in complex with a rat Mdm2 peptide. Determined by X-ray diffraction at 3.0 Å resolution. Released 19 Jul 2023.
Explore 8HSV in 3D Show helices and sheets RCSB PDB PDBe
8HSV contains 21 α-helices and 53 β-strands across 2 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 | 6-12 | 7 | 1 |
| β-strand | 19-22 | 4 | 1 |
| β-strand | 26-30 | 5 | 2 |
| β-strand | 33-34 | 2 | 2 |
| α-helix | 35-36 | 2 | |
| β-strand | 37-42 | 6 | 1 |
| β-strand | 52-63 | 12 | 3 |
| β-strand | 75-85 | 11 | 3 |
| α-helix | 95-97 | 3 | |
| α-helix | 99-108 | 10 | |
| β-strand | 112-117 | 6 | 1 |
| α-helix | 119-120 | 2 | |
| α-helix | 123-126 | 4 | |
| β-strand | 127-129 | 3 | 3 |
| β-strand | 140-151 | 12 | 3 |
| α-helix | 157-158 | 2 | |
| β-strand | 164-168 | 5 | 3 |
| β-strand | 169-172 | 4 | 2 |
| α-helix | 180-182 | 3 | |
| β-strand | 183-188 | 6 | 4 |
| β-strand | 197-202 | 6 | 4 |
| β-strand | 209 | 1 | 5 |
| β-strand | 214-222 | 9 | 4 |
| β-strand | 228 | 1 | 6 |
| β-strand | 231-241 | 11 | 7 |
| β-strand | 247-258 | 12 | 7 |
| β-strand | 262 | 1 | 6 |
| α-helix | 263 | 1 | |
| β-strand | 266-274 | 9 | 4 |
| α-helix | 279-281 | 3 | |
| β-strand | 289 | 1 | 3 |
| β-strand | 300 | 1 | 3 |
| α-helix | 301-305 | 5 | |
| β-strand | 317-328 | 12 | 7 |
| β-strand | 342-349 | 8 | 7 |
| β-strand | 352 | 1 | 5 |
| α-helix | 353-356 | 4 | |
| β-strand | 386-390 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-12 | 7 | 8 |
| β-strand | 18-22 | 5 | 8 |
| β-strand | 26-30 | 5 | 9 |
| β-strand | 33-34 | 2 | 9 |
| α-helix | 35-36 | 2 | |
| β-strand | 37-43 | 7 | 8 |
| β-strand | 52-63 | 12 | 10 |
| β-strand | 75-85 | 11 | 10 |
| α-helix | 99-106 | 8 | |
| β-strand | 112-117 | 6 | 8 |
| α-helix | 119-120 | 2 | |
| α-helix | 123-126 | 4 | |
| β-strand | 127-129 | 3 | 10 |
| β-strand | 140-151 | 12 | 10 |
| α-helix | 157-158 | 2 | |
| β-strand | 163-168 | 6 | 10 |
| β-strand | 169-173 | 5 | 9 |
| α-helix | 181-182 | 2 | |
| β-strand | 183-189 | 7 | 3 |
| β-strand | 196-203 | 8 | 3 |
| β-strand | 207-209 | 3 | 11 |
| β-strand | 214-222 | 9 | 3 |
| β-strand | 227-241 | 15 | 12 |
| β-strand | 247-258 | 12 | 12 |
| β-strand | 262 | 1 | 12 |
| β-strand | 266-274 | 9 | 3 |
| α-helix | 280-283 | 4 | |
| β-strand | 288-289 | 2 | 10 |
| β-strand | 300 | 1 | 10 |
| α-helix | 301-306 | 6 | |
| α-helix | 313-315 | 3 | |
| β-strand | 317-330 | 14 | 12 |
| β-strand | 342-349 | 8 | 12 |
| β-strand | 350-352 | 3 | 11 |
| α-helix | 353-355 | 3 | |
| β-strand | 386-390 | 5 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-arrestin-1 | A, B | protein | 414 | Rattus norvegicus | P29066 (AlphaFold model) |
| peptide from E3 ubiquitin-protein ligase Mdm2 | E, F | protein | 18 | Rattus norvegicus | D3ZVH5 (AlphaFold model) |
>8HSV_1 Beta-arrestin-1 (chains A, B) MGSSHHHHHHSSGLVPRGSHMGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVDPVDGV VLVDPEYLKERRVYVTLTVAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRL QERLIKKLGEHAYPFTFEIPPNLPSSVTLQPGPEDTGKALGVDYEVKAFVAENLEEKIHK RNSVRLVIRKVQYAPERPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHV TNNTNKTVKKIKISVRQYADIVLFNTAQYKVPVAMEEADDTVAPSSTFSKVYTLTPFLAN NREKRGLALDGKLKHEDTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLAS SDVAVELPFTLMHPKPKEEPPHREVPESETPVDTNLIELDTNDDDIVFEDFARQ
>8HSV_2 peptide from E3 ubiquitin-protein ligase Mdm2 (chains E, F) DLDDGVSDHSADCLDQDS
GPCR targeting of E3 ubiquitin ligase MDM2 by inactive beta-arrestin. Yun, Y., Yoon, H.J., Jeong, Y. et al. Proc Natl Acad Sci U S A (2023) 120:e2301934120-e2301934120. DOI 10.1073/pnas.2301934120 · PubMed
Other PDB entries of the same protein (UniProt P29066 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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