3twd

X-ray diffraction
1.9Å resolution

glmuC1 in complex with an antibacterial inhibitor

Released:

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
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
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: 222 amino acids
Theoretical weight: 23.5 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0ACC7 (Residues: 233-452; Coverage: 48%)
Gene names: JW3708, b3730, glmU, yieA
Sequence domains: Bacterial transferase hexapeptide (six repeats)
Structure domains: Hexapeptide repeat proteins

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P63
Unit cell:
a: 80.526Å b: 80.526Å c: 139.85Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
not available not available 0.217
Expression system: Escherichia coli