Fast maturing red fluorescent protein, DsRed.T4. Determined by X-ray diffraction at 1.64 Å resolution. Released 6 Nov 2007.
Explore 2VAE in 3D Show helices and sheets RCSB PDB PDBe
2VAE contains 60 α-helices and 106 β-strands across 8 chains. 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 | 12-22 | 11 | 1 |
| β-strand | 25-36 | 12 | 1 |
| β-strand | 41-50 | 10 | 1 |
| α-helix | 52 | 1 | |
| α-helix | 54 | 1 | |
| α-helix | 58-60 | 3 | |
| α-helix | 62-64 | 3 | |
| α-helix | 70-72 | 3 | |
| β-strand | 74 | 1 | 1 |
| α-helix | 82-85 | 4 | |
| β-strand | 91-99 | 9 | 1 |
| β-strand | 104-114 | 11 | 1 |
| β-strand | 117-127 | 11 | 1 |
| β-strand | 140-143 | 4 | 1 |
| α-helix | 144-145 | 2 | |
| β-strand | 146-153 | 8 | 1 |
| β-strand | 156-167 | 12 | 1 |
| β-strand | 172-183 | 12 | 1 |
| α-helix | 187-189 | 3 | |
| β-strand | 193-204 | 12 | 1 |
| β-strand | 210-220 | 11 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-22 | 11 | 2 |
| β-strand | 25-36 | 12 | 2 |
| β-strand | 41-50 | 10 | 2 |
| α-helix | 52 | 1 | |
| α-helix | 54 | 1 | |
| α-helix | 58-60 | 3 | |
| α-helix | 62-64 | 3 | |
| α-helix | 70-72 | 3 | |
| β-strand | 74 | 1 | 2 |
| α-helix | 82-85 | 4 | |
| β-strand | 91-99 | 9 | 2 |
| β-strand | 104-114 | 11 | 2 |
| β-strand | 117-127 | 11 | 2 |
| β-strand | 140-143 | 4 | 2 |
| α-helix | 144-145 | 2 | |
| β-strand | 146-153 | 8 | 2 |
| β-strand | 156-167 | 12 | 2 |
| β-strand | 172-183 | 12 | 2 |
| β-strand | 193-204 | 12 | 2 |
| β-strand | 210-220 | 11 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-22 | 11 | 3 |
| β-strand | 25-36 | 12 | 3 |
| β-strand | 41-50 | 10 | 3 |
| α-helix | 52 | 1 | |
| α-helix | 54 | 1 | |
| α-helix | 58-60 | 3 | |
| α-helix | 62-64 | 3 | |
| α-helix | 70-72 | 3 | |
| β-strand | 74 | 1 | 3 |
| α-helix | 82-85 | 4 | |
| β-strand | 91-99 | 9 | 3 |
| β-strand | 104-114 | 11 | 3 |
| β-strand | 117-127 | 11 | 3 |
| β-strand | 140-143 | 4 | 3 |
| α-helix | 144-145 | 2 | |
| β-strand | 146-153 | 8 | 3 |
| β-strand | 156-167 | 12 | 3 |
| β-strand | 172-183 | 12 | 3 |
| β-strand | 187 | 1 | 4 |
| α-helix | 188-189 | 2 | |
| β-strand | 193-204 | 12 | 3 |
| β-strand | 210-220 | 11 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-22 | 11 | 6 |
| β-strand | 25-36 | 12 | 6 |
| β-strand | 41-50 | 10 | 6 |
| α-helix | 52 | 1 | |
| α-helix | 54 | 1 | |
| α-helix | 58-60 | 3 | |
| α-helix | 62-64 | 3 | |
| α-helix | 70-72 | 3 | |
| β-strand | 74 | 1 | 6 |
| α-helix | 82-85 | 4 | |
| β-strand | 91-99 | 9 | 6 |
| β-strand | 104-114 | 11 | 6 |
| β-strand | 117-127 | 11 | 6 |
| β-strand | 140-143 | 4 | 6 |
| α-helix | 144-145 | 2 | |
| β-strand | 146-153 | 8 | 6 |
| β-strand | 156-167 | 12 | 6 |
| β-strand | 172-183 | 12 | 6 |
| β-strand | 187 | 1 | 4 |
| β-strand | 193-204 | 12 | 6 |
| β-strand | 210-220 | 11 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Red fluorescent protein | A, B, C, D, E, F, G, H | protein | 223 | DISCOSOMA SP. | Q9U6Y8 (AlphaFold model) |
>2VAE_1 RED FLUORESCENT PROTEIN (chains A, B, C, D, E, F, G, H) MASSEDVIKEFMRFKVRMEGSVNGHEFEIEGEGEGRPYEGTQTAKLKVTKGGPLPFAWDI LSPQFQYGSKVYVKHPADIPDYKKLSFPEGFKWERVMNFEDGGVVTVTQDSSLQDGCFIY KVKFIGVNFPSDGPVMQKKTMGWEPSTERLYPRDGVLKGEIHKALKLKDGGHYLVEFKSI YMAKKPVQLPGYYYVDSKLDITSHNEDYTIVEQYERAEGRHHLFL
Structural Rearrangements Near the Chromophore Influence the Maturation Speed and Brightness of Dsred Variants. Strongin, D.E., Bevis, B., Khuong, N. et al. Protein Eng Des Sel (2007) 20:525. DOI 10.1093/PROTEIN/GZM046 · PubMed
Other PDB entries of the same protein (UniProt Q9U6Y8 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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