Human erythropoietin, NMR minimized average structure. Determined by solution NMR. Released 10 Sept 1999.
Explore 1BUY in 3D Show helices and sheets RCSB PDB PDBe
1BUY contains 9 α-helices and 2 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 | 9-26 | 18 | |
| β-strand | 41 | 1 | 1 |
| α-helix | 48-51 | 4 | |
| α-helix | 56-83 | 28 | |
| α-helix | 92-111 | 20 | |
| α-helix | 132 | 1 | |
| β-strand | 133 | 1 | 1 |
| α-helix | 134 | 1 | |
| α-helix | 138-148 | 11 | |
| α-helix | 149-153 | 5 | |
| α-helix | 154-161 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (erythropoietin) | A | protein | 166 | Homo sapiens | P01588 (AlphaFold model) |
>1BUY_1 PROTEIN (ERYTHROPOIETIN) (chains A) APPRLICDSRVLERYLLEAKEAEKITTGCAEHCSLNEKITVPDTKVNFYAWKRMEVGQQA VEVWQGLALLSEAVLRGQALLVKSSQPWEPLQLHVDKAVSGLRSLTTLLRALGAQKEAIS PPDAASAAPLRTITADTFRKLFRVYSNFLRGKLKLYTGEACRTGDR
NMR structure of human erythropoietin and a comparison with its receptor bound conformation. Cheetham, J.C., Smith, D.M., Aoki, K.H. et al. Nat Struct Biol (1998) 5:861-866. DOI 10.1038/2302 · PubMed
Other PDB entries of the same protein (UniProt P01588 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1BUY 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.