› 5ec3

X-ray diffraction
2.1Å resolution

Structural insight into the catalyitc mechanism of human 4-Hydroxyphenylpyruvate dioxygenase

Released:
DOI: 10.2210/pdb5ec3/pdb
PDB entry 5ec3 coloured by chain, front view.
PDB entry 5ec3 coloured by chain, side view.
PDB entry 5ec3 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Yang WC, Yang GF

Function and Biology Details

Reaction catalysed: 
4-hydroxyphenylpyruvate + O(2) = homogentisate + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152436 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxyphenylpyruvate dioxygenase Chain: A
Molecule details ›
Chain: A
Length: 393 amino acids
Theoretical weight: 45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P32754 (Residues: 1-393; Coverage: 100%)
Gene names: HPD, PPD
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

1 bound ligand:
Ligand CO 1 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P3121
Unit cell:
a: 98.54Å b: 98.54Å c: 87.27Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.156 0.154 0.192
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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