3kdj

X-ray diffraction
1.88Å resolution

Complex structure of (+)-ABA-bound PYL1 and ABI1

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

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Abscisic acid receptor PYL1 Chain: A
Molecule details ›
Chain: A
Length: 202 amino acids
Theoretical weight: 23.33 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8VZS8 (Residues: 20-221; Coverage: 91%)
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
Protein phosphatase 2C 56 Chain: B
Molecule details ›
Chain: B
Length: 316 amino acids
Theoretical weight: 34.79 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49597 (Residues: 119-434; Coverage: 73%)
Gene names: ABI1, At4g26080, F20B18.190
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 61.61Å b: 86.788Å c: 110.701Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.246
Expression system: Escherichia coli BL21(DE3)