3kdi

X-ray diffraction
2.38Å resolution

Structure of (+)-ABA bound PYL2

Released:
Source organism: Arabidopsis thaliana
Primary publication:
Structural insights into the mechanism of abscisic acid signaling by PYL proteins.
Nat. Struct. Mol. Biol. 16 1230-6 (2009)
PMID: 19893533

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Abscisic acid receptor PYL2 Chain: A
Molecule details ›
Chain: A
Length: 190 amino acids
Theoretical weight: 21.31 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O80992 (Residues: 1-190; Coverage: 100%)
Gene names: At2g26040, PYL2, RCAR14, T19L18.15
Sequence domains: Polyketide cyclase / dehydrase and lipid transport
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P6122
Unit cell:
a: 60.922Å b: 60.922Å c: 253.382Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.226 0.281
Expression system: Escherichia coli BL21(DE3)