3d8v

X-ray diffraction
2.55Å resolution

Crystal structure of GlmU from Mycobacterium tuberculosis in complex with uridine-diphosphate-N-acetylglucosamine

Released:
Source organism: Mycobacterium tuberculosis
Primary publication:
Structure and function of GlmU from Mycobacterium tuberculosis.
Acta Crystallogr D Biol Crystallogr 65 275-83 (2009)
PMID: 19237750

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:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-161813 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chain: A
Molecule details ›
Chain: A
Length: 495 amino acids
Theoretical weight: 51.64 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WMN3 (Residues: 1-495; Coverage: 100%)
Gene names: Rv1018c, glmU
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: R32
Unit cell:
a: 114.238Å b: 114.238Å c: 361.796Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.199 0.244
Expression system: Escherichia coli