Ensemble of the solution structures of domain one of receptor associated protein. Determined by solution NMR. Released 6 Apr 2004.
Explore 1OV2 in 3D Show helices and sheets RCSB PDB PDBe
1OV2 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 | 23-35 | 13 | |
| α-helix | 39-65 | 27 | |
| α-helix | 72-88 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-2-macroglobulin receptor-associated protein precursor | A | protein | 99 | Homo sapiens | P30533 (AlphaFold model) |
>1OV2_1 Alpha-2-macroglobulin receptor-associated protein precursor (chains A) YSREKNQPKPSPKRESGEEFRMEKLNQLWEKAQRLHLPPVRLAELHADLKIQERDELAWK KLKLDGLDEDGEKEARLIRNLNVILAKYGLDGKKDARQV
1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein. Wu, Y., Migliorini, M., Yu, P. et al. J Biomol NMR (2003) 26:187-188. DOI 10.1023/A:1023534107920 · 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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