MolNFT v1 · #136381 · protein
1.5 a crystal structure of PYR1 bound to pyrabactin
5UR4 · Abscisic acid receptor PYR1: “1.5 a crystal structure of PYR1 bound to pyrabactin”. X-ray diffraction, 1 ligand (PYV), 2 pockets (best druggability 0.79). MolNFT v1 #136381 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5UR4
- Type
- protein
- Length
- 172 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Abscisic acid receptor PYR1
- UniProt
- O49686
- Ligands
- PYV
- Pockets
- 2 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Abscisic acid receptor PYR1 | protein | 172 | 27% helix, 38% strand | O49686 |
Ligands and binding sites
- PYV · 4-bromo-N-(pyridin-2-ylmethyl)naphthalene-1-sulfonamide · ligand · chains A
- GOL · Glycerol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 263 | 0.79 | 0.91 | 33 | PYV |
| 2 | 52 | 0.67 | 0.96 | 19 | empty |
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 O49686
- Elsewhere: RCSB PDB 5UR4 · PDBe 5UR4 · UniProt O49686
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