2LYH: Faap24 residues 141-215

Structure of Faap24 residues 141-215. Determined by solution NMR. Released 1 May 2013.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
576
Mol. weight
10.75 kDa
Released
1 May 2013

Explore 2LYH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 5 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix160-1634
α-helix174-1774
α-helix184-1885
α-helix192-1987
α-helix201-21212

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Fanconi anemia-associated protein of 24 kDaAprotein98Homo sapiensQ9BTP7 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2LYH_1 Fanconi anemia-associated protein of 24 kDa (chains A)
MGSSHHHHHHSSHMLVPRGSLEPSKNPLLGKKRALLLSEPSLLRTVQQIPGVGKVKAPLL
LQKFPSIQQLSNASIGELEQVVGQAVAQQIHAFFTQPR

Primary citation

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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