› 5or2

X-ray diffraction
2.5Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129275 (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
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

Ligands and Environments

2 bound ligands:
Ligand A4H 1 x A4H
Ligand MN 3 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OXFORD DIFFRACTION NOVA
Spacegroup: P212121
Unit cell:
a: 45.54Å b: 66.077Å c: 172.569Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.225 0.296
Expression system: Escherichia coli

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