Solution structure of human relaxin-3. Determined by solution NMR. Released 24 Jan 2006.
Explore 2FHW in 3D Show helices and sheets RCSB PDB PDBe
2FHW contains 3 α-helices and 2 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 |
|---|---|---|---|
| α-helix | 2-12 | 11 | |
| β-strand | 15-16 | 2 | 1 |
| α-helix | 17-21 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-7 | 2 | 1 |
| α-helix | 12-22 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7) | B | protein | 27 | Q8WXF3 (AlphaFold model) | |
| Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7) | A | protein | 24 | Q8WXF3 (AlphaFold model) |
>2FHW_1 Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7) (chains B) RAAPYGVRLCGREFIRAVIFTCGGSRW
>2FHW_2 Relaxin 3 (Prorelaxin H3) (Insulin-like peptide INSL7) (Insulin-like peptide 7) (chains A) DVLAGLSSSCCKWGCSKSEISSLC
Solution structure and novel insights into the determinants of the receptor specificity of human relaxin-3. Rosengren, K.J., Lin, F., Bathgate, R.A. et al. J Biol Chem (2006) 281:5845-5851. DOI 10.1074/jbc.M511210200 · PubMed
Other PDB entries of the same protein (UniProt Q8WXF3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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