Human lamin A coil 2B fragment. Determined by X-ray diffraction at 2.4 Å resolution. Released 9 Mar 2011.
Explore 2XV5 in 3D Show helices and sheets RCSB PDB PDBe
2XV5 contains 2 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 | 327-379 | 53 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lamin-a/c | A, B | protein | 74 | HOMO SAPIENS | P02545 (AlphaFold model) |
>2XV5_1 LAMIN-A/C (chains A, B) GGSARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEE ERLRLSPSPTSQRS
Simultaneous Formation of Right- and Left-Handed Anti-Parallel Coiled-Coil Interfaces by a Coil2 Fragment of Human Lamin A. Kapinos, L.E., Burkhard, P., Herrmann, H. et al. J Mol Biol (2011) 408:135. DOI 10.1016/J.JMB.2011.02.037 · 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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