NMR structure of FBP28 WW2 mutant Y438R, L453A DNDC. Determined by solution NMR. Released 3 Dec 2014.
Explore 2MWE in 3D Show helices and sheets RCSB PDB PDBe
2MWE contains 0 α-helices and 3 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 |
|---|---|---|---|
| β-strand | 436-440 | 5 | 1 |
| β-strand | 444-449 | 6 | 1 |
| β-strand | 454-456 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription elongation regulator 1 | A | protein | 28 | Homo sapiens | O14776 (AlphaFold model) |
>2MWE_1 Transcription elongation regulator 1 (chains A) SEWTERKTADGKTYYYNNRTAESTWEKP
Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements. Zhou, R., Maisuradze, G.G., Sunol, D. et al. Proc Natl Acad Sci U S A (2014) 111:18243-18248. DOI 10.1073/pnas.1420914111 · PubMed
Other PDB entries of the same protein (UniProt O14776 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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