Crystal structure of Ego3 mutant. Determined by X-ray diffraction at 2.6 Å resolution. Released 28 Nov 2012.
Explore 4FUW in 3D Show helices and sheets RCSB PDB PDBe
4FUW contains 10 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 | 19-23 | 5 | |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 36-41 | 6 | 1 |
| α-helix | 50-75 | 26 | |
| β-strand | 86-91 | 6 | 1 |
| β-strand | 94-102 | 9 | 1 |
| β-strand | 107-112 | 6 | 1 |
| β-strand | 118-124 | 7 | 1 |
| α-helix | 130-142 | 13 | |
| α-helix | 145-147 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-17 | 9 | |
| α-helix | 19-20 | 2 | |
| β-strand | 25-30 | 6 | 2 |
| β-strand | 36-41 | 6 | 2 |
| α-helix | 50-76 | 27 | |
| β-strand | 85-91 | 7 | 2 |
| β-strand | 94-103 | 10 | 2 |
| β-strand | 106-112 | 7 | 2 |
| β-strand | 118-124 | 7 | 2 |
| α-helix | 130-141 | 12 | |
| α-helix | 145-147 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein SLM4 | A, B | protein | 161 | Saccharomyces cerevisiae | P38247 (AlphaFold model) |
>4FUW_1 Protein SLM4 (chains A, B) MVMLHSKNVKGFLENTLKPYGSLQSSMIITATNGGILSYATSNNDVPKNSINEINSVNNL KMMSLLIKDKWSEDENDTEEQHSNSCYPVEIDSFKTKIYTYEMEDLHTCVAQIPNSDLLL LFIAEGSFPYGLLVIKIERAMRELTDLFGYKLGLEHHHHHH
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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