X-ray diffraction
2.1Å resolution

An improved model of the Trypanosoma brucei CTP synthase glutaminase domain:acivicin complex.


Function and Biology Details

Reaction catalysed:
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
CTP synthase Chain: A
Molecule details ›
Chain: A
Length: 273 amino acids
Theoretical weight: 30.76 KDa
Source organism: Trypanosoma brucei gambiense DAL972
Expression system: Escherichia coli BL21(DE3)
  • Canonical: C9ZI73 (Residues: 320-589; Coverage: 46%)
Gene name: TbgDal_I580
Sequence domains: Glutamine amidotransferase class-I
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 50.48Å b: 63.68Å c: 76.58Å
α: 90° β: 90° γ: 90°
R R work R free
0.193 0.191 0.235
Expression system: Escherichia coli BL21(DE3)