› 6f8y

X-ray diffraction
2.86Å resolution

Function and Biology Details

Reaction catalysed: 
L-threonine + ATP + HCO(3)(-) = L-threonylcarbamoyladenylate + diphosphate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194132 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonylcarbamoyl-AMP synthase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 345 amino acids
Theoretical weight: 38.2 KDa
Source organism: Pyrococcus abyssi GE5
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UYB2 (Residues: 2-340; Coverage: 100%)
Gene names: PAB1302, PYRAB15960, sua5
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand THR 4 x THR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: C2
Unit cell:
a: 152.23Å b: 142.38Å c: 103.86Å
α: 90° β: 101.8° γ: 90°
R-values:
R R work R free
0.191 0.188 0.252
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA.
Hori et al. (2018)
2 more

1 mention without citation

Structure-function analysis of Sua5 protein reveals novel functional motifs required for the biosynthesis of the universal t6A tRNA modification.
Pichard-Kostuch et al. (2018)