Proton NMR assignments and solution conformation of rantes, a chemokine of the cc type. Determined by solution NMR. Released 3 Jun 1995.
Explore 1RTN in 3D Show helices and sheets RCSB PDB PDBe
1RTN contains 4 α-helices and 8 β-strands across 2 chains. 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 | 8-10 | 3 | 1 |
| α-helix | 21-23 | 3 | |
| β-strand | 26-30 | 5 | 2 |
| β-strand | 38-42 | 5 | 2 |
| β-strand | 48-51 | 4 | 2 |
| α-helix | 58-65 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Rantes | A, B | protein | 68 | Homo sapiens | P13501 (AlphaFold model) |
>1RTN_1 RANTES (chains A, B) SPYSSDTTPCCFAYIARPLPRAHIKEYFYTSGKCSNPAVVFVTRKNRQVCANPEKKWVRE YINSLEMS
Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type. Skelton, N.J., Aspiras, F., Ogez, J. et al. Biochemistry (1995) 34:5329-5342. DOI 10.1021/bi00016a004 · PubMed
Other PDB entries of the same protein (UniProt P13501 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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