Lamin A 1-70 coil1A dimer stabilized by C-terminal capping. Determined by X-ray diffraction at 2.83 Å resolution. Released 2 Sept 2020.
Explore 6YSH in 3D Show helices and sheets RCSB PDB PDBe
6YSH contains 6 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 | 30-86 | 57 | |
| α-helix | 88-90 | 3 | |
| α-helix | 93-102 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prelamin-A/C,Microtubule-associated protein RP/EB family member 1 | A | protein | 83 | Homo sapiens | P02545 (AlphaFold model), Q15691 (AlphaFold model) |
| Prelamin-A/C,Microtubule-associated protein RP/EB family member 1 | B | protein | 81 | Homo sapiens | P02545 (AlphaFold model), Q15691 (AlphaFold model) |
>6YSH_1 Prelamin-A/C,Microtubule-associated protein RP/EB family member 1 (chains A) RITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVDFYFGKLRNIELIC QENEGENDPVLQRIVDILYATDE
>6YSH_2 Prelamin-A/C,Microtubule-associated protein RP/EB family member 1 (chains B) ITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVDFYFGKLRNIELICQ ENEGENDPVLQRIVDILYATD
Addressing the Molecular Mechanism of Longitudinal Lamin Assembly Using Chimeric Fusions. Stalmans, G., Lilina, A.V., Vermeire, P.J. et al. Cells (2020) 9. DOI 10.3390/cells9071633 · PubMed
Other PDB entries of the same protein (UniProt P02545 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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