Structure of a dystrophin ww domain fragment in complex with a beta-dystroglycan peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 23 Aug 2000.
Explore 1EG4 in 3D Show helices and sheets RCSB PDB PDBe
1EG4 contains 16 α-helices and 7 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 | 49-54 | 6 | |
| β-strand | 61-65 | 5 | 1 |
| β-strand | 71-75 | 5 | 1 |
| β-strand | 80-82 | 3 | 1 |
| α-helix | 86-94 | 9 | |
| α-helix | 95-98 | 4 | |
| α-helix | 104-118 | 15 | |
| α-helix | 121-123 | 3 | |
| α-helix | 126-135 | 10 | |
| β-strand | 144-146 | 3 | 2 |
| α-helix | 147-164 | 18 | |
| α-helix | 171-186 | 16 | |
| β-strand | 193-195 | 3 | 2 |
| α-helix | 196-205 | 10 | |
| α-helix | 211-222 | 12 | |
| β-strand | 229 | 1 | 3 |
| α-helix | 231-247 | 17 | |
| α-helix | 251-254 | 4 | |
| α-helix | 260-269 | 10 | |
| β-strand | 276 | 1 | 3 |
| α-helix | 278-286 | 9 | |
| α-helix | 294-304 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-12 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-dystroglycan | P | protein | 15 | Q14118 (AlphaFold model) | |
| Dystrophin | A | protein | 261 | Homo sapiens | P11532 (AlphaFold model) |
>1EG4_1 BETA-DYSTROGLYCAN (chains P) KNMTPYRSPPPYVPP
>1EG4_2 DYSTROPHIN (chains A) GPASQHFLSTSVQGPWERAISPNKVPYYINHETQTTCWDHPKMTELYQSLADLNNVRFSA YRTAMKLRRLQKALCLDLLSLSAACDALDQHNLKQNDQPMDILQIINCLTTIYDRLEQEH NNLVNVPLCVDMCLNWLLNVYDTGRTGRIRVLSFKTGIISLCKAHLEDKYRYLFKQVASS TGFCDQRRLGLLLHDSIQIPRQLGEVASFGGSNIEPSVRSCFQFANNKPEIEAALFLDWM RLEPQSMVWLPVLHRVAAAET
Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan. Huang, X., Poy, F., Zhang, R. et al. Nat Struct Biol (2000) 7:634-638. DOI 10.1038/77923 · 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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