9EC1: Human Dystrophin Spectrin Repeat 24
The Structure of Human Dystrophin Spectrin Repeat 24. Determined by X-ray diffraction at 2.14 Å resolution. Released 22 Apr 2026.
- Method
- X-ray diffraction
- Resolution
- 2.14 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 7,630
- Mol. weight
- 108.38 kDa
- Released
- 22 Apr 2026
Explore 9EC1 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9EC1 contains 55 α-helices and 0 β-strands across 8 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.
Chain A: 8 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-29 | 27 | |
| α-helix | 31-33 | 3 | |
| α-helix | 34-36 | 3 | |
| α-helix | 39-41 | 3 | |
| α-helix | 42-55 | 14 | |
| α-helix | 59-75 | 17 | |
| α-helix | 78-81 | 4 | |
| α-helix | 82-116 | 35 | |
Chain B: 8 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-29 | 28 | |
| α-helix | 31-33 | 3 | |
| α-helix | 34-36 | 3 | |
| α-helix | 39-41 | 3 | |
| α-helix | 42-55 | 14 | |
| α-helix | 59-76 | 18 | |
| α-helix | 79-81 | 3 | |
| α-helix | 82-115 | 34 | |
Chain C: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-29 | 27 | |
| α-helix | 31-33 | 3 | |
| α-helix | 34-36 | 3 | |
| α-helix | 39-55 | 17 | |
| α-helix | 59-75 | 17 | |
| α-helix | 78-81 | 4 | |
| α-helix | 82-115 | 34 | |
Chain D: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-29 | 27 | |
| α-helix | 31-33 | 3 | |
| α-helix | 34-36 | 3 | |
| α-helix | 39-41 | 3 | |
| α-helix | 42-55 | 14 | |
| α-helix | 59-76 | 18 | |
| α-helix | 82-116 | 35 | |
Chain E: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-29 | 28 | |
| α-helix | 31-33 | 3 | |
| α-helix | 34-36 | 3 | |
| α-helix | 39-41 | 3 | |
| α-helix | 42-55 | 14 | |
| α-helix | 59-76 | 18 | |
| α-helix | 82-115 | 34 | |
Chain F: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-29 | 27 | |
| α-helix | 31-33 | 3 | |
| α-helix | 34-36 | 3 | |
| α-helix | 39-55 | 17 | |
| α-helix | 59-75 | 17 | |
| α-helix | 82-115 | 34 | |
Chain G: 7 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-29 | 27 | |
| α-helix | 31-33 | 3 | |
| α-helix | 34-36 | 3 | |
| α-helix | 39-41 | 3 | |
| α-helix | 42-55 | 14 | |
| α-helix | 59-75 | 17 | |
| α-helix | 82-115 | 34 | |
Chain H: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-29 | 27 | |
| α-helix | 31-33 | 3 | |
| α-helix | 46-56 | 11 | |
| α-helix | 59-75 | 17 | |
| α-helix | 82-113 | 32 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Dystrophin | A, B, C, D, E, F, G, H | protein | 117 | Homo sapiens | P11532 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA
>9EC1_1 Dystrophin (chains A, B, C, D, E, F, G, H)
STGLERLQELQEATDELDLKLRQAEVIKGSWQPVGDLLIDSLQDHLEKVKALRGEIAPLK
ENVSHVNDLARQLTTLGIQLSPYNLSTLEDLNTRWKLLQVAVEDRVRQLHEAHRDFG
Primary citation
The atomic structure of human dystrophin spectrin-like repeat 24. Streeter, O., Shi, K., Bui, H. et al. Acta Crystallogr F Struct Biol Commun (2026) 82:184-193. DOI 10.1107/S2053230X26003262 · PubMed
Other PDB entries of the same protein (UniProt P11532 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9D58 1.94 Å, Human Dystrophin tandem calponin homology actin-binding domain crystallized in a…
- 1EG3 2.0 Å, Structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
- 1EG4 2.0 Å, Structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide
- 3UUN 2.3 Å, Crystal Structure of N-terminal first spectrin repeat of dystrophin
- 1DXX 2.6 Å, N-terminal Actin-binding Domain of Human Dystrophin
Browse structure collections
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