Crystal of Arrestin2-V2Rpp-3-Fab30 complex. Determined by X-ray diffraction at 2.49 Å resolution. Released 28 Jul 2021.
Explore 7DFC in 3D Show helices and sheets RCSB PDB PDBe
7DFC contains 25 α-helices and 70 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 | 73-87 | 15 | 4 |
| α-helix | 90 | 1 | |
| α-helix | 96-98 | 3 | |
| α-helix | 99-108 | 10 | |
| β-strand | 112-117 | 6 | 1 |
| α-helix | 118-120 | 3 | |
| α-helix | 124-126 | 3 | |
| β-strand | 127-129 | 3 | 4 |
| α-helix | 130-131 | 2 | |
| α-helix | 139-140 | 2 | |
| β-strand | 141-150 | 10 | 4 |
| β-strand | 163-168 | 6 | 4 |
| β-strand | 169-171 | 3 | 2 |
| β-strand | 183-188 | 6 | 5 |
| α-helix | 195-196 | 2 | |
| β-strand | 197-203 | 7 | 5 |
| β-strand | 207-209 | 3 | 6 |
| β-strand | 214-222 | 9 | 5 |
| β-strand | 228-243 | 16 | 7 |
| β-strand | 245-258 | 14 | 7 |
| β-strand | 262 | 1 | 7 |
| β-strand | 266-274 | 9 | 5 |
| α-helix | 279-281 | 3 | |
| β-strand | 288-290 | 3 | 4 |
| α-helix | 291-292 | 2 | |
| α-helix | 299 | 1 | |
| β-strand | 300 | 1 | 4 |
| α-helix | 301-304 | 4 | |
| β-strand | 316-329 | 14 | 7 |
| α-helix | 333-335 | 3 | |
| β-strand | 343-349 | 7 | 7 |
| β-strand | 350-352 | 3 | 6 |
| α-helix | 353-355 | 3 | |
| α-helix | 359-361 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 18-21 | 4 | 13 |
| β-strand | 26-27 | 2 | 14 |
| β-strand | 32-40 | 9 | 13 |
| α-helix | 44-46 | 3 | |
| β-strand | 47-54 | 8 | 15 |
| β-strand | 61-67 | 7 | 15 |
| β-strand | 72-75 | 4 | 15 |
| β-strand | 83-88 | 6 | 13 |
| β-strand | 93-99 | 7 | 13 |
| β-strand | 107-115 | 9 | 15 |
| β-strand | 122-125 | 4 | 15 |
| β-strand | 129-131 | 3 | 15 |
| β-strand | 132-133 | 2 | 14 |
| β-strand | 142-146 | 5 | 16 |
| α-helix | 150-152 | 3 | |
| β-strand | 153-154 | 2 | 16 |
| β-strand | 157-167 | 11 | 16 |
| β-strand | 173-176 | 4 | 17 |
| β-strand | 185-187 | 3 | 16 |
| α-helix | 188-190 | 3 | |
| β-strand | 191-192 | 2 | 16 |
| β-strand | 198-207 | 10 | 16 |
| β-strand | 217-222 | 6 | 17 |
| α-helix | 223-225 | 3 | |
| β-strand | 227-232 | 6 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17-19 | 3 | 8 |
| β-strand | 23-25 | 3 | 9 |
| β-strand | 32-38 | 7 | 8 |
| β-strand | 46-51 | 6 | 9 |
| β-strand | 58-62 | 5 | 9 |
| β-strand | 66-67 | 2 | 9 |
| α-helix | 68 | 1 | |
| β-strand | 75-80 | 6 | 8 |
| β-strand | 83-88 | 6 | 8 |
| β-strand | 98-103 | 6 | 9 |
| α-helix | 109 | 1 | |
| β-strand | 110-111 | 2 | 9 |
| β-strand | 116-118 | 3 | 9 |
| β-strand | 124 | 1 | 10 |
| β-strand | 127-131 | 5 | 11 |
| α-helix | 132-134 | 3 | |
| α-helix | 135-138 | 4 | |
| β-strand | 142-152 | 11 | 11 |
| β-strand | 153 | 1 | 10 |
| β-strand | 158-163 | 6 | 12 |
| β-strand | 167 | 1 | 12 |
| β-strand | 172-176 | 5 | 11 |
| β-strand | 186-195 | 10 | 11 |
| α-helix | 196-201 | 6 | |
| β-strand | 205-211 | 7 | 12 |
| β-strand | 214-222 | 9 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 349-351 | 3 | 4 |
| α-helix | 358-360 | 3 | |
| β-strand | 361-364 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-arrestin-1 | A | protein | 426 | Bos taurus | P17870 (AlphaFold model) |
| V2Rpp-3 | V | protein | 22 | synthetic construct | P30518 (AlphaFold model) |
| FAB30 light chain | L | protein | 227 | Mus musculus | |
| FAB30 heavy chain | H | protein | 249 | Mus musculus |
>7DFC_1 Beta-arrestin-1 (chains A) MGDKGTRVFKKASPNGKLTVYLGKRDFVDHIDLVEPVDGVVLVDPEYLKERRVYVTLTCA FRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFTFEIP PNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPERPGP QPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVRQYAD ICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLTPFLANNREKRGLALDGKLKHEDTNL ASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKPKEEP PHREVPEHETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKEEEEDGTGSPRLNDRLE HHHHHH
>7DFC_2 V2Rpp-3 (chains V) RTPPSLGPQDESCTTASSSLRK
>7DFC_3 FAB30 LIGHT CHAIN (chains L) MFVFSIATNAYASDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLL IYSASSLYSGVPSRFSGSRSGTDFTLTISSLQPEDFATYYCQQYKYVPVTFGQGTKVEIK RTVAAPSVFIFPPSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQD SKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
>7DFC_4 FAB30 HEAVY CHAIN (chains H) MFVFSIATNAYAEISEVQLVESGGGLVQPGGSLRLSCAASGFNVYSSSIHWVRQAPGKGL EWVASISSYYGYTYYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSRQFWYS GLDYWGQGTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGA LTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDK THHHHHHHH
Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2. He, Q.T., Xiao, P., Huang, S.M. et al. Nat Commun (2021) 12:2396-2396. DOI 10.1038/s41467-021-22731-x · PubMed
Other PDB entries of the same protein (UniProt P17870 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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