Human rantes, NMR, 13 structures. Determined by solution NMR. Released 14 Oct 1996.
Explore 1HRJ in 3D Show helices and sheets RCSB PDB PDBe
1HRJ contains 2 α-helices and 12 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 | 7-11 | 5 | 1 |
| β-strand | 24 | 1 | 2 |
| β-strand | 28-29 | 2 | 3 |
| β-strand | 39-42 | 4 | 3 |
| β-strand | 43 | 1 | 2 |
| β-strand | 48-50 | 3 | 3 |
| α-helix | 57-64 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human regulated upon activation normal T-cell expressed and secreted | A, B | protein | 68 | Homo sapiens | P13501 (AlphaFold model) |
>1HRJ_1 HUMAN REGULATED UPON ACTIVATION NORMAL T-CELL EXPRESSED AND SECRETED (chains A, B) SPYSSDTTPCCFAYIARPLPRAHIKEYFYTSGKCSNPAVVFVTRKNRQVCANPEKKWVRE YINSLEMS
The three-dimensional solution structure of RANTES. Chung, C.W., Cooke, R.M., Proudfoot, A.E. et al. Biochemistry (1995) 34:9307-9314. DOI 10.1021/bi00029a005 · 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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