X-ray diffraction
1.8Å resolution

Structural basis for inhibitor selectivity revealed by crystal structures of plant and mammalian 4-hydroxyphenylpyruvate dioxygenases


Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
4-hydroxyphenylpyruvate dioxygenase Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 46.78 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P93836 (Residues: 23-445; Coverage: 95%)
Gene names: At1g06570, F12K11.9, HPD, PDS1
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 77.4Å b: 83.6Å c: 63.5Å
α: 90° β: 102.5° γ: 90°
R R work R free
0.231 0.216 0.266
Expression system: Escherichia coli BL21(DE3)