› 4kpz

X-ray diffraction
2.09Å resolution

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D-glucosamine 1-phosphate
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155145 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chain: A
Molecule details ›
Chain: A
Length: 456 amino acids
Theoretical weight: 49.35 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P43889 (Residues: 1-456; Coverage: 100%)
Gene names: HI_0642, glmU
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand 1SF 1 x 1SF
Ligand SO4 6 x SO4
Ligand MG 2 x MG
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: R32
Unit cell:
a: 108.751Å b: 108.751Å c: 327.488Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.2 0.226
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The Transcriptional Regulatory Network of Corynebacterium pseudotuberculosis.
Parise et al. (2021)
3 other articles

1 mention without citation

Identification of Mtb GlmU Uridyltransferase Domain Inhibitors by Ligand-Based and Structure-Based Drug Design Approaches.
Singh et al. (2022)