solution structure of domain 3 of RAP. Determined by solution NMR. Released 9 May 2006.
Explore 2FTU in 3D Show helices and sheets RCSB PDB PDBe
2FTU contains 3 α-helices and 2 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 | 18-24 | 7 | |
| α-helix | 32-70 | 39 | |
| α-helix | 76-112 | 37 | |
| β-strand | 115 | 1 | 1 |
| β-strand | 117 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-2-macroglobulin receptor-associated protein, domain 3 | A | protein | 118 | Homo sapiens | P30533 (AlphaFold model) |
>2FTU_1 Alpha-2-macroglobulin receptor-associated protein, domain 3 (chains A) RVSHQGYSTEAEFEEPRVIDLWDLAQSANLTDKELEAFREELKHFEAKIEKHNHYQKQLE IAHEKLRHAESVGDGERVSRSREKHALLEGRTKELGYTVKKHLQDLSGRISRARHNEL
RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi. Lee, D., Walsh, J.D., Mikhailenko, I. et al. Mol Cell (2006) 22:423-430. DOI 10.1016/j.molcel.2006.04.011 · PubMed
Other PDB entries of the same protein (UniProt P30533 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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