› 1jvg

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reactions catalysed: 
UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-glucosamine
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate = diphosphate + UDP-N-acetyl-alpha-D-galactosamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172456 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylhexosamine pyrophosphorylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 522 amino acids
Theoretical weight: 58.84 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16222 (Residues: 1-522; Coverage: 100%)
Gene names: SPAG2, UAP1
Sequence domains: UTP--glucose-1-phosphate uridylyltransferase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand UD2 2 x UD2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 85.581Å b: 71.785Å c: 93.561Å
α: 90° β: 94.01° γ: 90°
R-values:
R R work R free
0.201 0.201 0.24
Expression system: Escherichia coli

Quick links

Citations

18 review citations

Function of alternative splicing.
Stamm et al. (2005)
17 more

1 mention without citation

Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture.
Peneff et al. (2001)