› 4aa7

X-ray diffraction
2Å 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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chains: A, B
Molecule details ›
Chains: A, B
Length: 231 amino acids
Theoretical weight: 24.72 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: P0ACC7 (Residues: 227-456; Coverage: 50%)
Gene names: JW3708, b3730, glmU, yieA
Sequence domains: Bacterial transferase hexapeptide (six repeats)
Structure domains: Hexapeptide repeat proteins

Ligands and Environments

2 bound ligands:
Ligand R82 2 x R82
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P63
Unit cell:
a: 80.713Å b: 80.713Å c: 140.061Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.179 0.177 0.221
Expression system: Escherichia coli K-12

Quick links

Citations

2 review citations

Viable screening targets related to the bacterial cell wall.
Silver LL. (2013)
1 more