› 5tk5

X-ray diffraction
1.88Å resolution

Crystal structure of human 3HAO with iron bound in the active site

Released:
DOI: 10.2210/pdb5tk5/pdb
PDB entry 5tk5 coloured by chain, front view.
PDB entry 5tk5 coloured by chain, side view.
PDB entry 5tk5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of human 3-hydroxyanthranilate 3,4-dioxygenase with native and non-native metals bound in the active site.
Pidugu LS, Neu H, Wong TL, Pozharski E, Molloy JL, Michel SL, Toth EA
Acta Crystallogr D Struct Biol 73 340-348 (2017)
PMID: 28375145

Function and Biology Details

Reaction catalysed: 
3-hydroxyanthranilate + O(2) = 2-amino-3-carboxymuconate semialdehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155567 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hydroxyanthranilate 3,4-dioxygenase Chain: A
Molecule details ›
Chain: A
Length: 290 amino acids
Theoretical weight: 32.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P46952 (Residues: 1-286; Coverage: 100%)
Gene name: HAAO
Sequence domains: 3-hydroxyanthranilic acid dioxygenase
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand FE 1 x FE
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P6522
Unit cell:
a: 57.076Å b: 57.076Å c: 415.871Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.203 0.203 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Observing 3-hydroxyanthranilate-3,4-dioxygenase in action through a crystalline lens.
Wang et al. (2020)
2 more

2 mentions without citation

Human ESC-Derived Chimeric Mouse Models of Huntington's Disease Reveal Cell-Intrinsic Defects in Glial Progenitor Cell Differentiation.
Osipovitch et al. (2019)
1 more