Human Urocortin 3. Determined by solution NMR. Released 1 Jan 2008.
Explore 2RMH in 3D Show helices and sheets RCSB PDB PDBe
2RMH contains 2 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 | 5-7 | 3 | |
| α-helix | 12-32 | 21 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Urocortin-3 | A | protein | 38 | Q969E3 (AlphaFold model) |
>2RMH_1 Urocortin-3 (chains A) FTLSLDVPTNIMNLLFNIAKAKNLRAQAAANAHLMAQI
Common and divergent structural features of a series of corticotropin releasing factor-related peptides. Grace, C.R.R., Perrin, M.H., Cantle, J.P. et al. J Am Chem Soc (2007) 129:16102-16114. DOI 10.1021/ja0760933 · PubMed
Other PDB entries of the same protein (UniProt Q969E3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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