2q37

X-ray diffraction
2.5Å resolution

Crystal structure of OHCU decarboxylase in the presence of (S)-allantoin

Released:
Source organism: Arabidopsis thaliana
Primary publication:
Structural and functional basis for (S)-allantoin formation in the ureide pathway.
J Biol Chem 282 23457-64 (2007)
PMID: 17567580

Function and Biology Details

Reactions catalysed:
5-hydroxyisourate + H(2)O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-192332 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uric acid degradation bifunctional protein TTL Chain: A
Molecule details ›
Chain: A
Length: 181 amino acids
Theoretical weight: 20.84 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9LVM5 (Residues: 1-161; Coverage: 50%)
Gene names: At5g58220, MCK7.9, TTL
Sequence domains: OHCU decarboxylase
Structure domains: Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A, null
Spacegroup: P3121
Unit cell:
a: 73.582Å b: 73.582Å c: 69.647Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 0.259
Expression system: Escherichia coli BL21(DE3)