Ff11-60. Determined by solution NMR. Released 11 Jan 2012.
Explore 2LKS in 3D Show helices and sheets RCSB PDB PDBe
2LKS contains 3 α-helices and 0 β-strands across 1 chain. 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 | 14-27 | 14 | |
| α-helix | 36-45 | 10 | |
| α-helix | 47-54 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Pre-mRNA-processing factor 40 homolog A | A | protein | 50 | Homo sapiens | O75400 (AlphaFold model) |
>2LKS_1 Pre-mRNA-processing factor 40 homolog A (chains A) GNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQ
Cross-Validation of the Structure of a Transiently Formed and Low Populated FF Domain Folding Intermediate Determined by Relaxation Dispersion NMR and CS-Rosetta. Barette, J., Velyvis, A., Religa, T.L. et al. J Phys Chem B (2012) 116:6637-6644. DOI 10.1021/jp209974f · PubMed
Other PDB entries of the same protein (UniProt O75400 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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