1OP1: Domain 1 of receptor associated protein

Solution NMR structure of domain 1 of receptor associated protein. Determined by solution NMR. Released 26 Aug 2003.

Method
Solution NMR
Organism
Homo sapiens
Chains
1
Atoms
680
Mol. weight
9.66 kDa
Released
26 Aug 2003

Explore 1OP1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1OP1 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.

Chain A: 3 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix23-3513
α-helix39-6527
α-helix72-8817

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-2-macroglobulin receptor-associated protein precursorAprotein82Homo sapiensP30533 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1OP1_1 Alpha-2-macroglobulin receptor-associated protein precursor (chains A)
GEEFRMEKLNQLWEKAQRLHLPPVRLAELHADLKIQERDELAWKKLKLDGLDEDGEKEAR
LIRNLNVILAKYGLDGKKDARQ

Primary citation

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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