› 6bum

X-ray diffraction
1.51Å resolution

Crystal structures of cyanuric acid hydrolase from Moorella thermoacetica

Released:
DOI: 10.2210/pdb6bum/pdb
PDB entry 6bum coloured by chain, front view.
PDB entry 6bum coloured by chain, side view.
PDB entry 6bum coloured by chain, top view.
Source organism: Moorella thermoacetica ATCC 39073
Primary publication:
Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.
Shi K, Cho S, Aukema KG, Lee T, Bera AK, Seffernick JL, Wackett LP, Aihara H
PLoS One 14 e0216979 (2019)
PMID: 31181074

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173891 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cyanuric acid amidohydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 363 amino acids
Theoretical weight: 38.48 KDa
Source organism: Moorella thermoacetica ATCC 39073
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2RGM7 (Residues: 1-367; Coverage: 99%)
Gene name: Moth_2120
Sequence domains: Amidohydrolase ring-opening protein (Amido_AtzD_TrzD)

Ligands and Environments

4 bound ligands:
Ligand MLI 4 x MLI
Ligand CA 4 x CA
Ligand PDO 24 x PDO
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P212121
Unit cell:
a: 81.44Å b: 88.69Å c: 204.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.127 0.126 0.141
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Cyanuric Acid Biodegradation via Biuret: Physiology, Taxonomy, and Geospatial Distribution.
Aukema et al. (2020)

2 mentions without citation

Crystal structures of Moorella thermoacetica cyanuric acid hydrolase reveal conformational flexibility and asymmetry important for catalysis.
Shi et al. (2019)
1 more