Human Urocortin 2. Determined by solution NMR. Released 1 Jan 2008.
Explore 2RMG in 3D Show helices and sheets RCSB PDB PDBe
2RMG 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 | 12-20 | 9 | |
| α-helix | 23-39 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Urocortin-2 | A | protein | 38 | Q96RP3 (AlphaFold model) |
>2RMG_1 Urocortin-2 (chains A) IVLSLDVPIGLLQILLEQARARAAREQATTNARILARV
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 Q96RP3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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