NMR structure of Neuromedin C in presence of SDS micelles. Determined by solution NMR. Released 14 Oct 2015.
Explore 2N0H in 3D Show helices and sheets RCSB PDB PDBe
2N0H contains 1 α-helix 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 | 5-9 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neuromedin C (NMC) | A | protein | 11 | Homo sapiens | P07492 (AlphaFold model) |
>2N0H_1 Neuromedin C (NMC) (chains A) GNHWAVGHLMX
Conformational ensembles of neuromedin C reveal a progressive coil-helix transition within a binding-induced folding mechanism. Adrover, M., Sanchis, P., Vilanova, B. et al. RSC Adv (2015) 5:83074-83088. DOI 10.1039/C5RA12753J
Other PDB entries of the same protein (UniProt P07492 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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