Structure of Faap24 residues 141-215. Determined by solution NMR. Released 1 May 2013.
Explore 2LYH in 3D Show helices and sheets RCSB PDB PDBe
2LYH contains 5 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 | 160-163 | 4 | |
| α-helix | 174-177 | 4 | |
| α-helix | 184-188 | 5 | |
| α-helix | 192-198 | 7 | |
| α-helix | 201-212 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Fanconi anemia-associated protein of 24 kDa | A | protein | 98 | Homo sapiens | Q9BTP7 (AlphaFold model) |
>2LYH_1 Fanconi anemia-associated protein of 24 kDa (chains A) MGSSHHHHHHSSHMLVPRGSLEPSKNPLLGKKRALLLSEPSLLRTVQQIPGVGKVKAPLL LQKFPSIQQLSNASIGELEQVVGQAVAQQIHAFFTQPR
The Fanconi anemia associated protein FAAP24 uses two substrate specific binding surfaces for DNA recognition. Wienk, H., Slootweg, J.C., Speerstra, S. et al. Nucleic Acids Res (2013) 41:6739-6749. DOI 10.1093/nar/gkt354 · PubMed
Other PDB entries of the same protein (UniProt Q9BTP7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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