MolNFT v1 · #81434 · protein
Crystal structure of aba receptor PYL10 (apo)
3UQH · Abscisic acid receptor PYL10: “Crystal structure of aba receptor PYL10 (apo)”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.89). MolNFT v1 #81434 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3UQH
- Type
- protein
- Length
- 314 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Abscisic acid receptor PYL10
- UniProt
- Q8H1R0
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.89
Structure
x-ray diffraction · 2 distinct chains · 26% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Abscisic acid receptor PYL10 | protein | 159 | 27% helix, 42% strand | Q8H1R0 |
| B | Abscisic acid receptor PYL10 | protein | 155 | 26% helix, 42% strand | Q8H1R0 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · chains 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 | 847 | 0.89 | 0.92 | 90 | empty |
Interfaces
1 interface between chains.
- A–B · 1027 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 Q8H1R0
- Elsewhere: RCSB PDB 3UQH · PDBe 3UQH · UniProt Q8H1R0
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