› 1g95

X-ray diffraction
2.33Å 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 domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188962 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chain: A
Molecule details ›
Chain: A
Length: 459 amino acids
Theoretical weight: 49.4 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97R46 (Residues: 1-459; Coverage: 100%)
Gene names: SP_0988, glmU
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM1A
Spacegroup: R32
Unit cell:
a: 94.91Å b: 94.91Å c: 279.94Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.228 0.228 0.303
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Cytoplasmic steps of peptidoglycan biosynthesis.
Barreteau et al. (2008)
11 more

3 mentions without citation

Structure-based prediction reveals capping motifs that inhibit β-helix aggregation.
Bryan et al. (2011)
2 more