Crystal structure of Arabidopsis thaliana 14-3-3 omega in complex with a phosphopeptide from the transcription factor BZR1. Determined by X-ray diffraction at 3.5 Å resolution. Released 15 Nov 2023.
Explore 8QTC in 3D Show helices and sheets RCSB PDB PDBe
8QTC contains 26 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 | 4-18 | 15 | |
| α-helix | 21-34 | 14 | |
| α-helix | 39-41 | 3 | |
| α-helix | 42-75 | 34 | |
| α-helix | 79-106 | 28 | |
| α-helix | 107-111 | 5 | |
| α-helix | 112-115 | 4 | |
| α-helix | 119-138 | 20 | |
| α-helix | 141-165 | 25 | |
| α-helix | 171-182 | 12 | |
| α-helix | 183-187 | 5 | |
| α-helix | 191-207 | 17 | |
| α-helix | 214-237 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-17 | 14 | |
| α-helix | 21-34 | 14 | |
| α-helix | 39-41 | 3 | |
| α-helix | 42-75 | 34 | |
| α-helix | 79-106 | 28 | |
| α-helix | 107-111 | 5 | |
| α-helix | 112-114 | 3 | |
| α-helix | 118-138 | 21 | |
| α-helix | 141-165 | 25 | |
| α-helix | 171-182 | 12 | |
| α-helix | 183-187 | 5 | |
| α-helix | 191-207 | 17 | |
| α-helix | 217-234 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| 14-3-3-like protein GF14 omega | A, B | protein | 240 | Arabidopsis thaliana | Q01525 (AlphaFold model) |
| Protein BRASSINAZOLE-RESISTANT 1 | C | protein | 5 | Arabidopsis thaliana |
>8QTC_1 14-3-3-like protein GF14 omega (chains A, B) MASGREEFVYMAKLAEQAERYEEMVEFMEKVSAAVDGDELTVEERNLLSVAYKNVIGARR ASWRIISSIEQKEESRGNDDHVTAIREYRSKIETELSGICDGILKLLDSRLIPAAASGDS KVFYLKMKGDYHRYLAEFKTGQERKDAAEHTLAAYKSAQDIANAELAPTHPIRLGLALNF SVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQD
>8QTC_2 Protein BRASSINAZOLE-RESISTANT 1 (chains C) SNSAP
| ID | Name | Formula | Copies |
|---|---|---|---|
| CO | Cobalt (II) ion | Co | 1 |
Water and common crystallization additives (SO4) are not listed.
Mechanistic Insights into the Function of 14-3-3 Proteins as Negative Regulators of Brassinosteroid Signaling in Arabidopsis. Obergfell, E., Hohmann, U., Moretti, A. et al. Plant Cell Physiol (2024) 65:1674-1688. DOI 10.1093/pcp/pcae056 · PubMed
Other PDB entries of the same protein (UniProt Q01525 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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