Research workbench
Crystal structure of native abscisic acid receptor PYL9 with aba
Analyse Crystal structure of native abscisic acid receptor PYL9 with aba in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OQU
- Type
- protein
- Length
- 331 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Abscisic acid receptor PYL9
- UniProt
- Q84MC7
- Ligands
- A8S
- Pockets
- 1 · best druggability 0.89
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Abscisic acid receptor PYL9 | protein | 166 | 28% helix, 36% strand | Q84MC7 |
| B | Abscisic acid receptor PYL9 | protein | 165 | 28% helix, 37% strand | Q84MC7 |
Ligands and binding sites
- A8S · (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 849 | 0.89 | 0.91 | 92 | A8S |
Interfaces
1 interface between chains.
- A–B · 796 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3OQU · Crystal structure of native abscisic acid receptor PYL9 with ABA · the same entry in another collection · chain A against A, TM-score 1.00
- Q84MC7 · AlphaFold monomer V2.0 prediction for abscisic acid receptor PYL9 (Q84MC7) · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q84MC7
- Elsewhere: RCSB PDB 3OQU · PDBe 3OQU · UniProt Q84MC7
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