3qn1

X-ray diffraction
1.8Å resolution

Crystal structure of the PYR1 Abscisic Acid receptor in complex with the HAB1 type 2C phosphatase catalytic domain

Released:

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Abscisic acid receptor PYR1 Chain: A
Molecule details ›
Chain: A
Length: 193 amino acids
Theoretical weight: 21.71 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: O49686 (Residues: 3-191; Coverage: 99%)
Gene names: ABIP6, At4g17870, PYR1, RCAR11, T6K21.50
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: 337 amino acids
Theoretical weight: 37.35 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9CAJ0 (Residues: 178-511; Coverage: 68%)
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: ESRF BEAMLINE ID14-4, ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 45.85Å b: 65.86Å c: 170.87Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.174 0.218
Expression system: Escherichia coli