Research workbench
Crystal structure of dimeric abscisic acid (aba) receptor pyrabactin resistance 1 (PYR1) with aba-bound closed-lid and aba-free open-lid subunits
Analyse Crystal structure of dimeric abscisic acid (aba) receptor pyrabactin resistance… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3K3K
- Type
- protein
- Length
- 366 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Abscisic acid receptor PYR1
- UniProt
- O49686
- Ligands
- A8S
- Pockets
- 4 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Abscisic acid receptor PYR1 | protein | 183 | 28% helix, 36% strand | O49686 |
| B | Abscisic acid receptor PYR1 | protein | 183 | 31% helix, 35% strand | O49686 |
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 · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 206 | 0.84 | 0.97 | 28 | A8S |
| 2 | 399 | 0.78 | 0.87 | 45 | empty |
| 3 | 114 | 0.39 | 0.75 | 22 | empty |
| 4 | 144 | 0.38 | 0.73 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 792 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3K3K · Crystal structure of dimeric abscisic acid (ABA) receptor pyrabactin resistance 1 (PYR1)… · the same entry in another collection · chain A against A, TM-score 1.00
- O49686 · AlphaFold monomer V2.0 prediction for abscisic acid receptor PYR1 (O49686) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 O49686
- Elsewhere: RCSB PDB 3K3K · PDBe 3K3K · UniProt O49686
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