Research workbench
Crystal structure of the abscisic receptor PYL2 mutant A93F in complex with pyrabactin
Analyse Crystal structure of the abscisic receptor PYL2 mutant A93F in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NMP
- Type
- protein
- Length
- 528 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Abscisic acid receptor PYL2
- UniProt
- O80992
- Ligands
- PYV
- Pockets
- 5 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Abscisic acid receptor PYL2 | protein | 176 | 28% helix, 36% strand | O80992 |
Ligands and binding sites
- PYV · 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1001 | 0.86 | 0.87 | 68 | PYV |
| 2 | 394 | 0.77 | 0.86 | 37 | PYV |
| 3 | 134 | 0.43 | 0.76 | 23 | empty |
| 4 | 189 | 0.43 | 0.73 | 38 | empty |
| 5 | 143 | 0.43 | 0.75 | 22 | empty |
Interfaces
2 interfaces between chains.
- A–B · 888 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 568 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 3NMP · Crystal structure of the abscisic receptor PYL2 mutant A93F in complex with pyrabactin · the same entry in another collection · chain A against A, TM-score 1.00
- O80992 · AlphaFold monomer V2.0 prediction for abscisic acid receptor PYL2 (O80992) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 O80992
- Elsewhere: RCSB PDB 3NMP · PDBe 3NMP · UniProt O80992
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