› 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 entry 6xj4 coloured by chain, front view.
PDB entry 6xj4 coloured by chain, side view.
PDB entry 6xj4 coloured by chain, top view.
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:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-104355 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triuret hydrolase TrtA 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 names: HBH1_00246, trtA
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)

1 mention without citation

Discovery of an ultraspecific triuret hydrolase (TrtA) establishes the triuret biodegradation pathway.
Tassoulas et al. (2021)