2yqs

X-ray diffraction
2.3Å resolution

Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the product-binding form

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-130802 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylglucosamine pyrophosphorylase Chain: A
Molecule details ›
Chain: A
Length: 486 amino acids
Theoretical weight: 54.73 KDa
Source organism: Candida albicans
Expression system: Escherichia coli
UniProt:
  • Canonical: O74933 (Residues: 1-486; Coverage: 100%)
Gene name: UAP1
Sequence domains: UTP--glucose-1-phosphate uridylyltransferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P212121
Unit cell:
a: 61.947Å b: 90.868Å c: 94.884Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.223
Expression system: Escherichia coli