3LGO: Gse1p, member of the GSE/EGO complex

Structure of Gse1p, member of the GSE/EGO complex. Determined by X-ray diffraction at 2.85 Å resolution. Released 4 Aug 2010.

Method
X-ray diffraction
Resolution
2.85 Å
Organism
Saccharomyces cerevisiae
Chains
1
Atoms
1,094
Mol. weight
19.56 kDa
Released
4 Aug 2010

Explore 3LGO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 3 helices, 8 β-strands

ElementResiduesLengthSheet
α-helix7-159
β-strand34-3961
β-strand45-4951
α-helix66-8116
β-strand9511
β-strand98-10032
β-strand103-10532
β-strand107-11151
β-strand116-12161
β-strand127-13371
α-helix139-15517

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein SLM4Aprotein172Saccharomyces cerevisiaeP38247 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3LGO_1 Protein SLM4 (chains A)
MGSSHHHHHHMVMLHSKNVKGFLENTLKPYDLHSVDFKTSSLQSSMIITATNGGILSYAT
SNNDVPKNSINEINSVNNLKMMSLLIKDKWSEDENDTEEQHSNSCYPVEIDSFKTKIYTY
EMEDLHTCVAQIPNSDLLLLFIAEGSFPYGLLVIKIERAMRELTDLFGYKLG

Primary citation

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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