› 4zdk

X-ray diffraction
3.49Å 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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161561 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CTP synthase Chains: A, B
Molecule details ›
Chains: A, B
Length: 586 amino acids
Theoretical weight: 63.71 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

4 bound ligands:
Ligand ONL 2 x ONL
Ligand ACP 2 x ACP
Ligand UTP 2 x UTP
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: I212121
Unit cell:
a: 121.732Å b: 194.724Å c: 207.457Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

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

4 mentions without citation

A multitarget approach to drug discovery inhibiting Mycobacterium tuberculosis PyrG and PanK.
Chiarelli et al. (2018)
3 more