Research workbench
Crystal structure of native abscisic acid receptor PYL3
Analyse Crystal structure of native abscisic acid receptor PYL3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KLX
- Type
- protein
- Length
- 361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F3N23.20 protein
- UniProt
- Q9SSM7
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F3N23.20 protein | protein | 180 | 29% helix, 37% strand | Q9SSM7 |
| B | F3N23.20 protein | protein | 181 | 28% helix, 34% strand | Q9SSM7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 767 | 0.86 | 0.88 | 68 | SO4 |
| 2 | 106 | 0.33 | 0.72 | 22 | empty |
| 3 | 69 | 0.29 | 0.73 | 17 | empty |
| 4 | 64 | 0.26 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 955 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
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 Q9SSM7
- Elsewhere: RCSB PDB 3KLX · PDBe 3KLX · UniProt Q9SSM7
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