Dimer Sgt2 from S.cerevisiae. Determined by solution NMR. Released 10 Dec 2025.
Explore 9LLV in 3D Show helices and sheets RCSB PDB PDBe
9LLV contains 29 α-helices and 0 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 | 5-22 | 18 | |
| α-helix | 27-44 | 18 | |
| α-helix | 51-57 | 7 | |
| α-helix | 98-114 | 17 | |
| α-helix | 118-131 | 14 | |
| α-helix | 136-148 | 13 | |
| α-helix | 152-165 | 14 | |
| α-helix | 170-181 | 12 | |
| α-helix | 187-200 | 14 | |
| α-helix | 201-203 | 3 | |
| α-helix | 206-222 | 17 | |
| α-helix | 236-238 | 3 | |
| α-helix | 271-274 | 4 | |
| α-helix | 312-315 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-22 | 16 | |
| α-helix | 27-44 | 18 | |
| α-helix | 52-55 | 4 | |
| α-helix | 91-93 | 3 | |
| α-helix | 95-97 | 3 | |
| α-helix | 98-113 | 16 | |
| α-helix | 118-129 | 12 | |
| α-helix | 136-148 | 13 | |
| α-helix | 152-165 | 14 | |
| α-helix | 170-183 | 14 | |
| α-helix | 186-195 | 10 | |
| α-helix | 196-200 | 5 | |
| α-helix | 206-222 | 17 | |
| α-helix | 253-256 | 4 | |
| α-helix | 310-315 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Small glutamine-rich tetratricopeptide repeat-containing protein 2 | A, B | protein | 347 | Saccharomyces cerevisiae S288C | Q12118 (AlphaFold model) |
>9LLV_1 Small glutamine-rich tetratricopeptide repeat-containing protein 2 (chains A, B) MSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEF KGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYEL AINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAK YAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDA SQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAE GFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQY
Remote on-off switching of protein activity by intrinsically disordered region. Ji, T., Ge, P., Zhang, S. et al. Nat Struct Mol Biol (2025) 32:2088-2098. DOI 10.1038/s41594-025-01585-7 · PubMed
Other PDB entries of the same protein (UniProt Q12118 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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