Solution structure of human prolactin. Determined by solution NMR. Released 22 Feb 2005.
Explore 1RW5 in 3D Show helices and sheets RCSB PDB PDBe
1RW5 contains 8 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-31 | 17 | |
| α-helix | 32-36 | 5 | |
| α-helix | 37-41 | 5 | |
| α-helix | 59-62 | 4 | |
| α-helix | 69-75 | 7 | |
| α-helix | 79-103 | 25 | |
| α-helix | 111-137 | 27 | |
| α-helix | 161-193 | 33 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prolactin | A | protein | 199 | Homo sapiens | P01236 (AlphaFold model) |
>1RW5_1 Prolactin (chains A) LPICPGGAARCQVTLRDLFDRAVVLSHYIHNLSSEMFSEFDKRYTHGRGFITKAINSCHT SSLATPEDKEQAQQMNQKDFLSLIVSILRSWNEPLYHLVTEVRGMQEAPEAILSKAVEIE EQTKRLLEGMELIVSQVHPETKENEIYPVWSGLPSLQMADEESRLSAYYNLLHCLRRDSH KIDNYLKLLKCRIIHNNNC
Solution structure of human prolactin. Teilum, K., Hoch, J.C., Goffin, V. et al. J Mol Biol (2005) 351:810-823. DOI 10.1016/j.jmb.2005.06.042 · PubMed
Other PDB entries of the same protein (UniProt P01236 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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