Crystal structure of HY5 leucine zipper homodimer from Arabidopsis thaliana. Determined by X-ray diffraction at 2.0 Å resolution. Released 20 Mar 2007.
Explore 2OQQ in 3D Show helices and sheets RCSB PDB PDBe
2OQQ contains 2 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 | 3-41 | 39 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-41 | 40 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription factor HY5 | A, B | protein | 42 | Arabidopsis thaliana | O24646 (AlphaFold model) |
>2OQQ_1 Transcription factor HY5 (chains A, B) GSAYLSELENRVKDLENKNSELEERLSTLQNENQMLRHILKN
Structural basis for the conformational integrity of the Arabidopsis thaliana HY5 leucine zipper homodimer. Yoon, M.K., Kim, H.M., Choi, G. et al. J Biol Chem (2007) 282:12989-13002. DOI 10.1074/jbc.M611465200 · PubMed
Other PDB entries of the same protein (UniProt O24646 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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