Crystal structure of Ego3 homodimer. Determined by X-ray diffraction at 2.1 Å resolution. Released 28 Nov 2012.
Explore 4FTX in 3D Show helices and sheets RCSB PDB PDBe
4FTX contains 12 α-helices and 12 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 9-17 | 9 | |
| α-helix | 22-24 | 3 | |
| β-strand | 34-39 | 6 | 1 |
| β-strand | 45-50 | 6 | 1 |
| α-helix | 59-84 | 26 | |
| β-strand | 94-100 | 7 | 1 |
| β-strand | 103-112 | 10 | 1 |
| β-strand | 115-121 | 7 | 1 |
| α-helix | 122 | 1 | |
| β-strand | 127-134 | 8 | 1 |
| α-helix | 139-150 | 12 | |
| α-helix | 151-156 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-16 | 8 | |
| α-helix | 22-24 | 3 | |
| β-strand | 34-39 | 6 | 1 |
| β-strand | 45-50 | 6 | 1 |
| α-helix | 59-84 | 26 | |
| β-strand | 94-100 | 7 | 1 |
| β-strand | 103-112 | 10 | 1 |
| β-strand | 115-121 | 7 | 1 |
| α-helix | 122 | 1 | |
| β-strand | 127-133 | 7 | 1 |
| α-helix | 139-150 | 12 | |
| α-helix | 151-156 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein SLM4 | A, B | protein | 170 | Saccharomyces cerevisiae | P38247 (AlphaFold model) |
>4FTX_1 Protein SLM4 (chains A, B) MVMLHSKNVKGFLENTLKPYDLHSVDFKTSSLQSSMIITATNGGILSYATSNNDVPKNSI NEINSVNNLKMMSLLIKDKWSEDENDTEEQHSNSCYPVEIDSFKTKIYTYEMEDLHTCVA QIPNSDLLLLFIAEGSFPYGLLVIKIERAMRELTDLFGYKLGLEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| SIN | Succinic acid | C4 H6 O4 | 1 |
Ego3 functions as a homodimer to mediate the interaction between Gtr1-Gtr2 and Ego1 in the ego complex to activate TORC1. Zhang, T., Peli-Gulli, M.P., Yang, H. et al. Structure (2012) 20:2151-2160. DOI 10.1016/j.str.2012.09.019 · PubMed
Other PDB entries of the same protein (UniProt P38247 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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