NMR structure of the first RRM domain of the protein RBM39 from Homo sapiens. Determined by solution NMR. Released 1 Jan 2014.
Explore 2MHN in 3D Show helices and sheets RCSB PDB PDBe
2MHN contains 3 α-helices and 5 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 | 7-11 | 5 | |
| β-strand | 14-18 | 5 | 1 |
| α-helix | 27-34 | 8 | |
| β-strand | 39-42 | 4 | 1 |
| β-strand | 56-61 | 6 | 1 |
| α-helix | 66-71 | 6 | |
| β-strand | 78 | 1 | 2 |
| β-strand | 81 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA-binding protein 39 | A | protein | 94 | Homo sapiens | Q14498 (AlphaFold model) |
>2MHN_1 RNA-binding protein 39 (chains A) GHMNLTPEERDARTVFCMQLAARIRPRDLEEFFSTVGKVRDVRMISDRNSRRSKGIAYVE FVDVSSVPLAIGLTGQRVLGVPIIVQASQAEKNR
NMR structure of the first RRM domain of the protein RBM39 from Homo sapiens. Serrano, P., Wuthrich, K., Geralt, M. et al. To be published.
Other PDB entries of the same protein (UniProt Q14498 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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