3foq

X-ray diffraction
3.41Å resolution

Crystal structure of N-acetylglucosamine-1-phosphate uridyltransferase (GlmU) from Mycobacterium tuberculosis in a cubic space group.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional protein GlmU Chain: A
Molecule details ›
Chain: A
Length: 503 amino acids
Theoretical weight: 52.73 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WMN3 (Residues: 1-495; Coverage: 100%)
Gene names: Rv1018c, glmU
Sequence domains: MobA-like NTP transferase domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I432
Unit cell:
a: 285.7Å b: 285.7Å c: 285.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.287 0.285 0.321
Expression system: Escherichia coli