The structure of receptor-associated protein(RAP). Determined by solution NMR. Released 21 Aug 2007.
Explore 2P03 in 3D Show helices and sheets RCSB PDB PDBe
2P03 contains 10 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 | 23-35 | 13 | |
| α-helix | 39-65 | 27 | |
| α-helix | 72-88 | 17 | |
| α-helix | 115-127 | 13 | |
| α-helix | 133-161 | 29 | |
| α-helix | 184-209 | 26 | |
| α-helix | 223-230 | 8 | |
| α-helix | 237-274 | 38 | |
| α-helix | 275-277 | 3 | |
| α-helix | 283-315 | 33 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-2-macroglobulin receptor-associated protein | A | protein | 323 | Homo sapiens | P30533 (AlphaFold model) |
>2P03_1 Alpha-2-macroglobulin receptor-associated protein (chains A) YSREKNQPKPSPKRESGEEFRMEKLNQLWEKAQRLHLPPVRLAELHADLKIQERDELAWK KLKLDGLDEDGEKEARLIRNLNVILAKYGLDGKKDARQVTSNSLSGTQEDGLDDPRLEKL WHKAKTSGKFSGEELDKLWREFLHHKEKVHEYNVLLETLSRTEEIHENVISPSDLSDIKG SVLHSRHTELKEKLRSINQGLDRLRRVSHQGYSTEAEFEEPRVIDLWDLAQSANLTDKEL EAFREELKHFEAKIEKHNHYQKQLEIAHEKLRHAESVGDGERVSRSREKHALLEGRTKEL GYTVKKHLQDLSGRISRARHNEL
The structure of receptor-associated protein (RAP). Lee, D., Walsh, J.D., Migliorini, M. et al. Protein Sci (2007) 16:1628-1640. DOI 10.1110/ps.072865407 · 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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