Beta-arrestin 1 mutant S13D/T275D. Determined by X-ray diffraction at 2.79 Å resolution. Released 29 Jan 2020.
Explore 6KL7 in 3D Show helices and sheets RCSB PDB PDBe
6KL7 contains 19 α-helices and 59 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 | 26-29 | 4 | 2 |
| β-strand | 34 | 1 | 2 |
| β-strand | 37-42 | 6 | 1 |
| β-strand | 52-63 | 12 | 3 |
| β-strand | 75-87 | 13 | 3 |
| α-helix | 96-98 | 3 | |
| α-helix | 99-108 | 10 | |
| β-strand | 112-117 | 6 | 1 |
| α-helix | 124-126 | 3 | |
| β-strand | 127-130 | 4 | 3 |
| α-helix | 136-138 | 3 | |
| β-strand | 140-151 | 12 | 3 |
| α-helix | 160-162 | 3 | |
| β-strand | 163-168 | 6 | 3 |
| β-strand | 169-172 | 4 | 2 |
| α-helix | 175-177 | 3 | |
| α-helix | 180-184 | 5 | |
| β-strand | 185-189 | 5 | 4 |
| β-strand | 191 | 1 | 5 |
| β-strand | 197-203 | 7 | 4 |
| β-strand | 207-209 | 3 | 6 |
| β-strand | 214-222 | 9 | 4 |
| β-strand | 228-241 | 14 | 7 |
| β-strand | 247-258 | 12 | 7 |
| β-strand | 262 | 1 | 7 |
| α-helix | 263 | 1 | |
| β-strand | 266-274 | 9 | 4 |
| α-helix | 278-280 | 3 | |
| β-strand | 287-289 | 3 | 3 |
| β-strand | 295 | 1 | 8 |
| β-strand | 300 | 1 | 3 |
| α-helix | 301-304 | 4 | |
| β-strand | 317-329 | 13 | 7 |
| β-strand | 342-349 | 8 | 7 |
| β-strand | 350-352 | 3 | 6 |
| α-helix | 353-355 | 3 | |
| β-strand | 386-390 | 5 | 1 |
| α-helix | 393-394 | 2 | |
| β-strand | 395 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-11 | 5 | 9 |
| β-strand | 19-22 | 4 | 9 |
| β-strand | 26-29 | 4 | 10 |
| β-strand | 34 | 1 | 10 |
| β-strand | 37-38 | 2 | 11 |
| β-strand | 39-42 | 4 | 9 |
| β-strand | 54-63 | 10 | 12 |
| β-strand | 75-85 | 11 | 12 |
| α-helix | 99-105 | 7 | |
| β-strand | 116-117 | 2 | 11 |
| α-helix | 124-126 | 3 | |
| β-strand | 127-130 | 4 | 12 |
| β-strand | 140-149 | 10 | 12 |
| β-strand | 164-168 | 5 | 12 |
| β-strand | 169-172 | 4 | 10 |
| α-helix | 181-184 | 4 | |
| β-strand | 185-189 | 5 | 13 |
| β-strand | 197-203 | 7 | 13 |
| β-strand | 207-209 | 3 | 14 |
| β-strand | 214-222 | 9 | 13 |
| β-strand | 228-241 | 14 | 15 |
| β-strand | 245 | 1 | 5 |
| β-strand | 247-258 | 12 | 15 |
| β-strand | 262 | 1 | 15 |
| β-strand | 266-274 | 9 | 13 |
| α-helix | 278-280 | 3 | |
| β-strand | 287-289 | 3 | 12 |
| β-strand | 295 | 1 | 16 |
| β-strand | 300 | 1 | 12 |
| α-helix | 301-305 | 5 | |
| β-strand | 317-329 | 13 | 15 |
| β-strand | 342-349 | 8 | 15 |
| β-strand | 350-352 | 3 | 14 |
| α-helix | 353-355 | 3 | |
| β-strand | 387-390 | 4 | 9 |
| α-helix | 393-394 | 2 | |
| β-strand | 395 | 1 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-arrestin-1 | A, B | protein | 422 | Rattus norvegicus | P29066 (AlphaFold model) |
>6KL7_1 Beta-arrestin-1 (chains A, B) GSHMMGDKGTRVFKKADPNGKLTVYLGKRDFVDHIDLVDPVDGVVLVDPEYLKERRVYVT LTCAFRYGREDLDVLGLTFRKDLFVANVQSFPPAPEDKKPLTRLQERLIKKLGEHAYPFT FEIPPNLPCSVTLQPGPEDTGKACGVDYEVKAFCAENLEEKIHKRNSVRLVIRKVQYAPE RPGPQPTAETTRQFLMSDKPLHLEASLDKEIYYHGEPISVNVHVTNNTNKTVKKIKISVR QYADICLFNTAQYKCPVAMEEADDTVAPSSTFCKVYTLDPFLANNREKRGLALDGKLKHE DTNLASSTLLREGANREILGIIVSYKVKVKLVVSRGGLLGDLASSDVAVELPFTLMHPKP KEEPPHREVPESETPVDTNLIELDTNDDDIVFEDFARQRLKGMKDDKDEEDDGTGSPHLN NR
| ID | Name | Formula | Copies |
|---|---|---|---|
| BA | Barium ion | Ba | 5 |
Water and common crystallization additives (EDO) are not listed.
Conformational Dynamics and Functional Implications of Phosphorylated beta-Arrestins. Kang, H., Yang, H.S., Ki, A.Y. et al. Structure (2020) 28:314. DOI 10.1016/j.str.2019.12.008 · PubMed
Other PDB entries of the same protein (UniProt P29066 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6KL7 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.