3jrq

X-ray diffraction
2.1Å resolution

Crystal structure of (+)-ABA-bound PYL1 in complex with ABI1

Released:

Function and Biology Details

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein phosphatase 2C 56 Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 35.88 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: P49597 (Residues: 125-429; Coverage: 70%)
Gene names: ABI1, At4g26080, F20B18.190
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
Abscisic acid receptor PYL1 Chain: B
Molecule details ›
Chain: B
Length: 186 amino acids
Theoretical weight: 21.45 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8VZS8 (Residues: 28-210; Coverage: 83%)
Gene names: At5g46790, MZA15.21, PYL1, RCAR12
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: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 49.01Å b: 60.62Å c: 84.96Å
α: 90° β: 104.56° γ: 90°
R-values:
R R work R free
0.201 0.198 0.249
Expression system: Escherichia coli