Solution structure of a novel Ubiquitin-binding domain from Human PLAA (PFUC, Gly76-Pro77 cis isomer). Determined by solution NMR. Released 5 May 2009.
Explore 2K89 in 3D Show helices and sheets RCSB PDB PDBe
2K89 contains 2 α-helices and 4 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 |
|---|---|---|---|
| β-strand | 57-59 | 3 | 1 |
| β-strand | 62-64 | 3 | 1 |
| β-strand | 66-70 | 5 | 2 |
| β-strand | 79-83 | 5 | 2 |
| α-helix | 89-100 | 12 | |
| α-helix | 106-118 | 13 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Phospholipase A-2-activating protein | A | protein | 80 | Homo sapiens | Q9Y263 (AlphaFold model) |
>2K89_1 Phospholipase A-2-activating protein (chains A) ANQQTSGKVLYEGKEFDYVFSIDVNEGGPSYKLPYNTSDDPWLTAYNFLQKNDLNPMFLD QVAKFIIDNTKGQMLGLGNP
Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A2-activating Protein. Fu, Q.S., Zhou, C.J., Gao, H.C. et al. J Biol Chem (2009) 284:19043-19052. DOI 10.1074/jbc.M109.009126 · PubMed
Other PDB entries of the same protein (UniProt Q9Y263 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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