2FTU: Domain 3 of RAP

solution structure of domain 3 of RAP. Determined by solution NMR. Released 9 May 2006.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
978
Mol. weight
13.88 kDa
Released
9 May 2006

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

Secondary structure: helices and β-sheets

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.

Chain A: 3 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix18-247
α-helix32-7039
α-helix76-11237
β-strand11511
β-strand11711

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-2-macroglobulin receptor-associated protein, domain 3Aprotein118Homo sapiensP30533 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2FTU_1 Alpha-2-macroglobulin receptor-associated protein, domain 3 (chains A)
RVSHQGYSTEAEFEEPRVIDLWDLAQSANLTDKELEAFREELKHFEAKIEKHNHYQKQLE
IAHEKLRHAESVGDGERVSRSREKHALLEGRTKELGYTVKKHLQDLSGRISRARHNEL

Primary citation

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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