Crystal structure of EGO-TC. Determined by X-ray diffraction at 2.4 Å resolution. Released 5 Aug 2015.
Explore 4XPM in 3D Show helices and sheets RCSB PDB PDBe
4XPM contains 11 α-helices and 15 β-strands across 3 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 | 154-171 | 18 | |
| β-strand | 181-182 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 11-16 | 6 | 2 |
| β-strand | 21-26 | 6 | 2 |
| α-helix | 27-30 | 4 | |
| α-helix | 32-34 | 3 | |
| α-helix | 35-38 | 4 | |
| α-helix | 41-43 | 3 | |
| β-strand | 48-52 | 5 | 2 |
| β-strand | 56-63 | 8 | 2 |
| β-strand | 66-73 | 8 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-4 | 2 | 1 |
| α-helix | 6-16 | 11 | |
| α-helix | 18-20 | 3 | |
| β-strand | 21 | 1 | 3 |
| β-strand | 28 | 1 | 3 |
| α-helix | 29-32 | 4 | |
| β-strand | 34-39 | 6 | 4 |
| β-strand | 45-50 | 6 | 4 |
| α-helix | 66-83 | 18 | |
| β-strand | 94-100 | 7 | 4 |
| β-strand | 103-112 | 10 | 4 |
| β-strand | 115-121 | 7 | 4 |
| β-strand | 127-134 | 8 | 4 |
| α-helix | 139-151 | 13 | |
| α-helix | 154-156 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein MEH1 | A | protein | 39 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q02205 (AlphaFold model) |
| Uncharacterized protein YCR075W-A | B | protein | 76 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q3E830 (AlphaFold model) |
| Protein SLM4 | C | protein | 162 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P38247 (AlphaFold model) |
>4XPM_1 Protein MEH1 (chains A) SPDSAKISKEQLKKLHSNILNEIFSQSQVNKPGPLTVPF
>4XPM_2 Uncharacterized protein YCR075W-A (chains B) SMEAEKQSDIKGTIAFDTHGNVIESTGVGSQRIEDIGDLSKVTLDAEGFAQVQGDSLLVH LYKRNDITLAVYTSAQ
>4XPM_3 Protein SLM4 (chains C) MVMLHSKNVKGFLENTLKPYDLHSVDFKTSSLQSSMIITATNGGILSYATSNNDVPKNSI NEINSVNNLKMMSLLIKDKWSEDENDTEEQHSNSCYPVEIDSFKTKIYTYEMEDLHTCVA QIPNSDLLLLFIAEGSFPYGLLVIKIERAMRELTDLFGYKLG
Crystal structure of the Ego1-Ego2-Ego3 complex and its role in promoting Rag GTPase-dependent TORC1 signaling. Powis, K., Zhang, T., Panchaud, N. et al. Cell Res (2015) 25:1043-1059. DOI 10.1038/cr.2015.86 · PubMed
Other PDB entries of the same protein (UniProt Q02205 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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