Crystal Structure of AnkB Ankyrin Repeats R13-24 in complex with autoinhibition segment AI-c. Determined by X-ray diffraction at 1.95 Å resolution. Released 13 Sept 2017.
Explore 5Y4F in 3D Show helices and sheets RCSB PDB PDBe
5Y4F contains 51 α-helices and 2 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 | 433-440 | 8 | |
| α-helix | 443-451 | 9 | |
| α-helix | 466-472 | 7 | |
| α-helix | 476-484 | 9 | |
| α-helix | 494-496 | 3 | |
| α-helix | 499-505 | 7 | |
| α-helix | 509-517 | 9 | |
| α-helix | 532-539 | 8 | |
| α-helix | 542-550 | 9 | |
| α-helix | 565-572 | 8 | |
| α-helix | 575-583 | 9 | |
| α-helix | 598-604 | 7 | |
| α-helix | 608-616 | 9 | |
| α-helix | 631-638 | 8 | |
| α-helix | 641-649 | 9 | |
| α-helix | 664-671 | 8 | |
| α-helix | 674-682 | 9 | |
| β-strand | 690 | 1 | 1 |
| β-strand | 696 | 1 | 1 |
| α-helix | 697-704 | 8 | |
| α-helix | 707-715 | 9 | |
| α-helix | 730-737 | 8 | |
| α-helix | 740-748 | 9 | |
| α-helix | 763-769 | 7 | |
| α-helix | 773-781 | 9 | |
| α-helix | 796-802 | 7 | |
| α-helix | 806-813 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 433-440 | 8 | |
| α-helix | 443-451 | 9 | |
| α-helix | 466-473 | 8 | |
| α-helix | 476-484 | 9 | |
| α-helix | 494-496 | 3 | |
| α-helix | 499-505 | 7 | |
| α-helix | 509-517 | 9 | |
| α-helix | 532-539 | 8 | |
| α-helix | 542-550 | 9 | |
| α-helix | 565-572 | 8 | |
| α-helix | 575-583 | 9 | |
| α-helix | 598-604 | 7 | |
| α-helix | 608-616 | 9 | |
| α-helix | 631-637 | 7 | |
| α-helix | 641-649 | 9 | |
| α-helix | 664-671 | 8 | |
| α-helix | 674-682 | 9 | |
| α-helix | 697-703 | 7 | |
| α-helix | 707-715 | 9 | |
| α-helix | 730-737 | 8 | |
| α-helix | 740-748 | 9 | |
| α-helix | 763-769 | 7 | |
| α-helix | 773-781 | 9 | |
| α-helix | 796-803 | 8 | |
| α-helix | 806-812 | 7 | |
| α-helix | 826-828 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ankyrin-2 | A, B | protein | 444 | Homo sapiens | Q01484 (AlphaFold model) |
>5Y4F_1 Ankyrin-2 (chains A, B) SGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGAL VDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVL LEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQ KVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLA SQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGY TPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNA TTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEE GDDTMTGDGGEYLRPEDLKELGDD
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (ACT) are not listed.
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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