Crystal Structure of a Double Variant (W67L/W91H) of Recombinant Human Serum Retinol-binding Protein at 2.0 A Resolution. Determined by X-ray diffraction at 2.0 Å resolution. Released 1 Jul 2003.
Explore 1JYJ in 3D Show helices and sheets RCSB PDB PDBe
1JYJ contains 3 α-helices and 11 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 |
|---|---|---|---|
| β-strand | 5 | 1 | 1 |
| α-helix | 6-8 | 3 | |
| α-helix | 17-20 | 4 | |
| β-strand | 22-30 | 9 | 2 |
| β-strand | 37-47 | 11 | 2 |
| β-strand | 53-64 | 12 | 2 |
| β-strand | 67-79 | 13 | 2 |
| β-strand | 85-92 | 8 | 2 |
| β-strand | 100-109 | 10 | 2 |
| β-strand | 114-123 | 10 | 2 |
| β-strand | 128 | 1 | 1 |
| β-strand | 129-138 | 10 | 2 |
| α-helix | 146-158 | 13 | |
| β-strand | 166-167 | 2 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Plasma retinol-binding protein | A | protein | 183 | Homo sapiens | P02753 (AlphaFold model) |
>1JYJ_1 PLASMA RETINOL-BINDING PROTEIN (chains A) MERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKG RVRLLNNLDVCADMVGTFTDTEDPAKFKMKYHGVASFLQKGNDDHWIVDTDYDTYAVQYS CRLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYCDGRSE RNL
Role of Conserved Residues in Structure and Stability: Tryptophans of Human Serum Retinol-Binding Protein, a Model for the Lipocalin Superfamily. Greene, L.H., Chrysina, E.D., Irons, L.I. et al. Protein Sci (2001) 10:2301-2316. DOI 10.1110/ps.22901 · PubMed
Other PDB entries of the same protein (UniProt P02753 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1JYJ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.