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Crystal structure of the high-affinity abscisic acid receptor PYL9/RCAR9 bound to aba

Analyse Crystal structure of the high-affinity abscisic acid receptor PYL9/RCAR9 bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3W9R
Type
protein
Length
171 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Abscisic acid receptor PYL9
UniProt
Q84MC7
Ligands
A8S
Pockets
1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAbscisic acid receptor PYL9protein17131% helix, 37% strandQ84MC7

Ligands and binding sites

  • A8S · (2Z,4E)-5-[(1S)-1-hydroxy-2,6,6-trimethyl-4-oxocyclohex-2-en-1-yl]-3-methylpenta-2,4-dienoic acid · ligand · chains A
  • P6G · Hexaethylene glycol · additive · chains A

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13140.820.9241A8S, P6G

Compared structures

  • 3W9R · Crystal structure of the high-affinity abscisic acid receptor PYL9/RCAR9 bound to ABA · the same entry in another collection · chain A against A, TM-score 1.00
  • Q84MC7 · AlphaFold monomer V2.0 prediction for abscisic acid receptor PYL9 (Q84MC7) · a predicted model of the same protein · chain A against A, TM-score 0.93

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