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3iwv

X-ray diffraction
1.68Å resolution

Crystal structure of Y116T mutant of 5-HYDROXYISOURATE HYDROLASE (TRP)

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate + H(+).
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-170428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-hydroxyisourate hydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 138 amino acids
Theoretical weight: 15.44 KDa
Source organism: Danio rerio
Expression system: Escherichia coli
UniProt:
  • Canonical: Q06S87 (Residues: 1-138; Coverage: 100%)
Gene name: urah
Sequence domains: HIUase/Transthyretin family
Structure domains: Transthyretin/hydroxyisourate hydrolase domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 45.92Å b: 103.69Å c: 52.63Å
α: 90° β: 108.81° γ: 90°
R-values:
R R work R free
0.206 0.203 0.26
Expression system: Escherichia coli