Structure of Gse1p, member of the GSE/EGO complex. Determined by X-ray diffraction at 2.85 Å resolution. Released 4 Aug 2010.
Explore 3LGO in 3D Show helices and sheets RCSB PDB PDBe
3LGO contains 3 α-helices and 8 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 | 7-15 | 9 | |
| β-strand | 34-39 | 6 | 1 |
| β-strand | 45-49 | 5 | 1 |
| α-helix | 66-81 | 16 | |
| β-strand | 95 | 1 | 1 |
| β-strand | 98-100 | 3 | 2 |
| β-strand | 103-105 | 3 | 2 |
| β-strand | 107-111 | 5 | 1 |
| β-strand | 116-121 | 6 | 1 |
| β-strand | 127-133 | 7 | 1 |
| α-helix | 139-155 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein SLM4 | A | protein | 172 | Saccharomyces cerevisiae | P38247 (AlphaFold model) |
>3LGO_1 Protein SLM4 (chains A) MGSSHHHHHHMVMLHSKNVKGFLENTLKPYDLHSVDFKTSSLQSSMIITATNGGILSYAT SNNDVPKNSINEINSVNNLKMMSLLIKDKWSEDENDTEEQHSNSCYPVEIDSFKTKIYTY EMEDLHTCVAQIPNSDLLLLFIAEGSFPYGLLVIKIERAMRELTDLFGYKLG
Structural conservation of components in the amino acid sensing branch of the TOR pathway in yeast and mammals. Kogan, K., Spear, E.D., Kaiser, C.A. et al. J Mol Biol (2010) 402:388-398. DOI 10.1016/j.jmb.2010.07.034 · 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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