Crystal structure of wildtype dystroglycan proteolytic domain (juxtamembrane domain). Determined by X-ray diffraction at 2.43 Å resolution. Released 11 Sept 2024.
Explore 8UF4 in 3D Show helices and sheets RCSB PDB PDBe
8UF4 contains 23 α-helices and 36 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 |
|---|---|---|---|
| α-helix | 493-497 | 5 | |
| β-strand | 498-499 | 2 | 1 |
| β-strand | 505-509 | 5 | 2 |
| β-strand | 514-517 | 4 | 3 |
| α-helix | 518-519 | 2 | |
| β-strand | 523-525 | 3 | 1 |
| β-strand | 529-530 | 2 | 1 |
| α-helix | 531-533 | 3 | |
| β-strand | 535-539 | 5 | 2 |
| β-strand | 552-555 | 4 | 3 |
| β-strand | 560-563 | 4 | 3 |
| α-helix | 567-569 | 3 | |
| β-strand | 571-580 | 10 | 2 |
| β-strand | 586-596 | 11 | 2 |
| α-helix | 597-598 | 2 | |
| β-strand | 606-612 | 7 | 4 |
| α-helix | 617-620 | 4 | |
| α-helix | 623-636 | 14 | |
| β-strand | 645-651 | 7 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 655-661 | 7 | 4 |
| α-helix | 671-681 | 11 | |
| β-strand | 682 | 1 | 5 |
| α-helix | 687 | 1 | |
| β-strand | 688 | 1 | 5 |
| α-helix | 689 | 1 | |
| α-helix | 690-696 | 7 | |
| β-strand | 702-709 | 8 | 4 |
| α-helix | 711-713 | 3 | |
| β-strand | 717-719 | 3 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 499 | 1 | 6 |
| β-strand | 505-509 | 5 | 7 |
| β-strand | 514-517 | 4 | 8 |
| α-helix | 518-519 | 2 | |
| β-strand | 523 | 1 | 6 |
| β-strand | 524 | 1 | 9 |
| β-strand | 530 | 1 | 9 |
| β-strand | 535-539 | 5 | 7 |
| β-strand | 545 | 1 | 7 |
| α-helix | 546-547 | 2 | |
| β-strand | 552-555 | 4 | 8 |
| β-strand | 560-563 | 4 | 8 |
| α-helix | 567-569 | 3 | |
| β-strand | 571-580 | 10 | 7 |
| β-strand | 586-596 | 11 | 7 |
| α-helix | 597-598 | 2 | |
| β-strand | 606-612 | 7 | 10 |
| α-helix | 617-620 | 4 | |
| α-helix | 623-636 | 14 | |
| β-strand | 645-652 | 8 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| a-dystroglycan | A, C | protein | 163 | Homo sapiens | Q14118 (AlphaFold model) |
| Beta-dystroglycan | B, D | protein | 95 | Homo sapiens | Q14118 (AlphaFold model) |
>8UF4_1 a-dystroglycan (chains A, C) GEPNQRPELKNHIDRVDAWVGTYFEVKIPSDTFYDHEDTTTDKLKLTLKLREQQLVGEKS WVQFNSNSQLMYGLPDSSHVGKHEYFMHATDKGGLSAVDAFEIHVHRRPQGDRAPARFKA KFVGDPALVLNDIHKKIALVKKLAFAFGDRNCSTITLQNITRG
>8UF4_2 Beta-dystroglycan (chains B, D) SIVVEWTNNTLPLEPCPKEQIAGLSRRIAEDDGKPRPAFSNALEPDFKATSITVTGSGSC RHLQFIPVVPPRRVPSEAPPTEVPDRDPEKSSEDD
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (CL) are not listed.
Molecular basis of proteolytic cleavage regulation by the extracellular matrix receptor dystroglycan. Anderson, M.J.M., Hayward, A.N., Smiley, A.T. et al. Structure (2024) 32:1984-1996.e5. DOI 10.1016/j.str.2024.08.019 · PubMed
Other PDB entries of the same protein (UniProt Q14118 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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