Crystal Structure of AnkB Ankyrin Repeats R8-14 in complex with autoinhibition segment AI-b. Determined by X-ray diffraction at 2.34 Å resolution. Released 13 Sept 2017.
Explore 5Y4E in 3D Show helices and sheets RCSB PDB PDBe
5Y4E contains 29 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 1269-1275 | 7 | |
| α-helix | 1279-1287 | 9 | |
| α-helix | 1302-1308 | 7 | |
| α-helix | 1312-1320 | 9 | |
| α-helix | 1335-1341 | 7 | |
| α-helix | 1345-1353 | 9 | |
| α-helix | 1368-1375 | 8 | |
| α-helix | 1378-1386 | 9 | |
| α-helix | 1396-1398 | 3 | |
| α-helix | 1401-1407 | 7 | |
| α-helix | 1411-1419 | 9 | |
| α-helix | 1434-1441 | 8 | |
| α-helix | 1444-1452 | 9 | |
| α-helix | 1467-1473 | 7 | |
| α-helix | 1477-1487 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1269-1276 | 8 | |
| α-helix | 1279-1287 | 9 | |
| α-helix | 1302-1308 | 7 | |
| α-helix | 1312-1320 | 9 | |
| α-helix | 1335-1341 | 7 | |
| α-helix | 1345-1353 | 9 | |
| α-helix | 1368-1375 | 8 | |
| α-helix | 1378-1386 | 9 | |
| α-helix | 1401-1407 | 7 | |
| α-helix | 1411-1419 | 9 | |
| α-helix | 1434-1441 | 8 | |
| α-helix | 1444-1452 | 9 | |
| α-helix | 1467-1473 | 7 | |
| α-helix | 1477-1486 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ankyrin-2,Ankyrin-2 | A, B | protein | 277 | Homo sapiens | Q01484 (AlphaFold model) |
>5Y4E_1 Ankyrin-2,Ankyrin-2 (chains A, B) DGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSLVPRGSGSRNGITPLHVASK RGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSP LHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARA LNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGA SPDVTNIRGETALHMAARAGQVEVVRCLKVVTEEVTT
Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions. Chen, K., Li, J., Wang, C. et al. Elife (2017) 6. DOI 10.7554/eLife.29150 · PubMed
Other PDB entries of the same protein (UniProt Q01484 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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