Receptor associated protein (RAP) domain 1, NMR, 20 structures. Determined by solution NMR. Released 20 Aug 1997.
Explore 1LRE in 3D Show helices and sheets RCSB PDB PDBe
1LRE 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) |
>1LRE_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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