Crystal structure of the coiled-coil surrounding Skip 2 of MYH7. Determined by X-ray diffraction at 2.55 Å resolution. Released 1 Jul 2015.
Explore 4XA3 in 3D Show helices and sheets RCSB PDB PDBe
4XA3 contains 8 α-helices and 0 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 | 5-16 | 12 | |
| α-helix | 22-230 | 109 | |
| α-helix | 237-245 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| α-helix | 5-16 | 12 | |
| α-helix | 22-1374 | 42 | |
| α-helix | 1376-230 | 66 | |
| α-helix | 238-243 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Gp7-MYH7(1361-1425)-Eb1 chimera protein | A, B | protein | 154 | Bacillus phage phi29, Homo sapiens | P12883 (AlphaFold model), P13848, Q15691 (AlphaFold model) |
>4XA3_1 Gp7-MYH7(1361-1425)-Eb1 chimera protein (chains A, B) GASMPLKPEEHEDILNKLLDPELAQSERTEALQQLRVNYGSFVSEYNDLTKSLSKANSEV AQWRTKYETDAIQRTEELEEAKKKLAQRLQEAEEAVEAVNAKCSSLEKTKHRLQNEIDFY FGKLRNIELICQENEGENDPVLQRIVDILYATDE
Skip residues modulate the structural properties of the myosin rod and guide thick filament assembly. Taylor, K.C., Buvoli, M., Korkmaz, E.N. et al. Proc Natl Acad Sci U S A (2015) 112:E3806-E3815. DOI 10.1073/pnas.1505813112 · PubMed
Other PDB entries of the same protein (UniProt P12883 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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