Receptor associated protein (RAP) domain 1, NMR, minimized average structure. Determined by solution NMR. Released 20 Aug 1997.
Explore 1NRE in 3D Show helices and sheets RCSB PDB PDBe
1NRE contains 3 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 | 23-34 | 12 | |
| α-helix | 39-65 | 27 | |
| α-helix | 73-88 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Receptor-associated protein | A | protein | 81 | Homo sapiens | P30533 (AlphaFold model) |
>1NRE_1 RECEPTOR-ASSOCIATED PROTEIN (chains A) GEEFRMEKLNQLWEKAQRLHLPPVRLAELHADLKIQERDELAWKKLKLDGLDEDGEKEAR LIRNLNVILAKYGLDGKKDAR
The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein. Nielsen, P.R., Ellgaard, L., Etzerodt, M. et al. Proc Natl Acad Sci U S A (1997) 94:7521-7525. DOI 10.1073/pnas.94.14.7521 · 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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