3kb3

X-ray diffraction
1.95Å resolution

Crystal structure of abscisic acid-bound PYL2 in complex with HAB1

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Abscisic acid receptor PYL2 Chain: A
Molecule details ›
Chain: A
Length: 176 amino acids
Theoretical weight: 19.85 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: O80992 (Residues: 14-188; Coverage: 92%)
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
Protein phosphatase 2C 16 Chain: B
Molecule details ›
Chain: B
Length: 321 amino acids
Theoretical weight: 35.53 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9CAJ0 (Residues: 186-506; Coverage: 66%)
Gene names: At1g72770, F28P22.4, HAB1, P2C-HA
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: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 60.319Å b: 67.466Å c: 143.905Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.214 0.259
Expression system: Escherichia coli