NMR structure of the FF domain L24A mutant's folding transition state. Determined by solution NMR. Released 28 Sept 2011.
Explore 2L9V in 3D Show helices and sheets RCSB PDB PDBe
2L9V contains 4 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 | 36-44 | 9 | |
| α-helix | 47-49 | 3 | |
| α-helix | 50-58 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Pre-mRNA-processing factor 40 homolog A | A | protein | 70 | Homo sapiens | O75400 (AlphaFold model) |
>2L9V_1 Pre-mRNA-processing factor 40 homolog A (chains A) SQPAKKTYTWNTKEEAKQAFKEALKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQA FNAYKVQTEK
Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study. Korzhnev, D.M., Vernon, R.M., Religa, T.L. et al. J Am Chem Soc (2011) 133:10974-10982. DOI 10.1021/ja203686t · 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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