N-terminal Actin-binding Domain of Human Dystrophin. Determined by X-ray diffraction at 2.6 Å resolution. Released 16 May 2000.
Explore 1DXX in 3D Show helices and sheets RCSB PDB PDBe
1DXX contains 64 α-helices and 4 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 | 14-31 | 18 | |
| α-helix | 48-58 | 11 | |
| α-helix | 70-86 | 17 | |
| α-helix | 96-100 | 5 | |
| α-helix | 104-115 | 12 | |
| α-helix | 116-120 | 5 | |
| α-helix | 122-131 | 10 | |
| α-helix | 136-148 | 13 | |
| α-helix | 161-163 | 3 | |
| α-helix | 167-176 | 10 | |
| α-helix | 178-180 | 3 | |
| α-helix | 183-187 | 5 | |
| α-helix | 192-201 | 10 | |
| α-helix | 202-206 | 5 | |
| α-helix | 215-218 | 4 | |
| α-helix | 225-236 | 12 | |
| β-strand | 243-245 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dystrophin | A, B, C, D | protein | 246 | HOMO SAPIENS | P11532 (AlphaFold model) |
>1DXX_1 DYSTROPHIN (chains A, B, C, D) MLWWEEVEDSYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQ KLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQV KNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDL FDWNSVVSQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLP QQVSIE
The Structure of the N-Terminal Actin-Binding Domain of Human Dystrophin and How Mutations in This Domain May Cause Duchenne or Becker Muscular Dystrophy. Norwood, F.L., Sutherland-Smith, A.J., Keep, N.H. et al. Structure (2000) 8:481. DOI 10.1016/S0969-2126(00)00132-5 · PubMed
Other PDB entries of the same protein (UniProt P11532 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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