› 4zdi

X-ray diffraction
3.52Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CTP synthase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 587 amino acids
Theoretical weight: 63.77 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WHK7 (Residues: 1-586; Coverage: 100%)
Gene names: MTCI125.21, Rv1699, pyrG
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CA 8 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P43
Unit cell:
a: 196.826Å b: 196.826Å c: 184.047Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.213 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 review citations

Molecular Targets Related Drug Resistance Mechanisms in MDR-, XDR-, and TDR-Mycobacterium tuberculosis Strains.
Hameed et al. (2018)
13 more

1 mention without citation

The pathogenic mechanism of Mycobacterium tuberculosis: implication for new drug development.
Yan et al. (2022)