Research workbench
Crystal structure of abscisic acid receptor PYL2
Analyse Crystal structure of abscisic acid receptor PYL2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KAZ
- Type
- protein
- Length
- 526 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein AT2G26040
- UniProt
- O80992
- Pockets
- 4 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative uncharacterized protein AT2G26040 | protein | 175 | 28% helix, 37% strand | O80992 |
| C | Putative uncharacterized protein AT2G26040 | protein | 176 | 28% helix, 37% strand | O80992 |
Ligands and binding sites
- BU2 · 1,3-butanediol · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 869 | 0.86 | 0.88 | 71 | BU2 |
| 2 | 368 | 0.76 | 0.86 | 40 | BU2 |
| 3 | 239 | 0.52 | 0.76 | 43 | empty |
| 4 | 223 | 0.45 | 0.73 | 45 | empty |
Interfaces
2 interfaces between chains.
- A–B · 938 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 577 Ų buried · 8 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 O80992
- Elsewhere: RCSB PDB 3KAZ · PDBe 3KAZ · UniProt O80992
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.