1DXX: Dystrophin

N-terminal Actin-binding Domain of Human Dystrophin. Determined by X-ray diffraction at 2.6 Å resolution. Released 16 May 2000.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
HOMO SAPIENS
Chains
4
Atoms
7,622
Mol. weight
113.84 kDa
Released
16 May 2000

Explore 1DXX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A, B, C and D: 16 helices, 1 β-strand

ElementResiduesLengthSheet
α-helix14-3118
α-helix48-5811
α-helix70-8617
α-helix96-1005
α-helix104-11512
α-helix116-1205
α-helix122-13110
α-helix136-14813
α-helix161-1633
α-helix167-17610
α-helix178-1803
α-helix183-1875
α-helix192-20110
α-helix202-2065
α-helix215-2184
α-helix225-23612
β-strand243-24531

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
DystrophinA, B, C, Dprotein246HOMO SAPIENSP11532 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>1DXX_1 DYSTROPHIN (chains A, B, C, D)
MLWWEEVEDSYEREDVQKKTFTKWVNAQFSKFGKQHIENLFSDLQDGRRLLDLLEGLTGQ
KLPKEKGSTRVHALNNVNKALRVLQNNNVDLVNIGSTDIVDGNHKLTLGLIWNIILHWQV
KNVMKNIMAGLQQTNSEKILLSWVRQSTRNYPQVNVINFTTSWSDGLALNALIHSHRPDL
FDWNSVVSQQSATQRLEHAFNIARYQLGIEKLLDPEDVDTTYPDKKSILMYITSLFQVLP
QQVSIE

Primary citation

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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