4bvs

X-ray diffraction
2.6Å resolution

Cyanuric acid hydrolase: evolutionary innovation by structural concatenation.

Released:

Function and Biology Details

Reaction catalysed:
Cyanuric acid + H(2)O = 1-carboxybiuret
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-157672 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyanuric acid amidohydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 40.42 KDa
Source organism: Pseudomonas sp. ADP
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P58329 (Residues: 1-363; Coverage: 100%)
Gene names: AOX63_31675, atzD
Sequence domains: Amidohydrolase ring-opening protein (Amido_AtzD_TrzD)
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: R32
Unit cell:
a: 128.365Å b: 128.365Å c: 228.412Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.177 0.216
Expression system: Escherichia coli BL21