› 6xj4

X-ray diffraction
1.78Å resolution

Triuret Hydrolase (TrtA) from Herbaspirillum sp. BH-1 C162S bound with biuret

Released:
DOI: 10.2210/pdb6xj4/pdb
PDB 6xj4 coloured by chain and viewed from the front.
PDB 6xj4 coloured by chain and viewed from the side.
PDB 6xj4 coloured by chain and viewed from the top.
Source organism: Herbaspirillum sp. BH-1
Primary publication:
Discovery of an ultraspecific triuret hydrolase (TrtA) establishes the triuret biodegradation pathway.
Tassoulas LJ, Elias MH, Wackett LP
J Biol Chem 296 100055
PMID: 33172891

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isochorismatase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 223 amino acids
Theoretical weight: 24.2 KDa
Source organism: Herbaspirillum sp. BH-1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A2N6JFX7 (Residues: 1-220; Coverage: 97%)
Gene name: HBH1_00246
Sequence domains: Isochorismatase family

Ligands and Environments

2 bound ligands:
Ligand EDO 5 x EDO
Ligand C5J 1 x C5J
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 51.63Å b: 114.18Å c: 141.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.156 0.187
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 citations in other articles

Filling in the Gaps in Metformin Biodegradation: a New Enzyme and a Metabolic Pathway for Guanylurea.
Tassoulas et al. (2021)