› 1vm8

X-ray diffraction
2.5Å resolution

Crystal structure of UDP-N-acetylglucosamine pyrophosphorylase (Agx2) from Mus musculus at 2.50 A resolution

Released:
DOI: 10.2210/pdb1vm8/pdb
PDB entry 1vm8 coloured by chain, front view.
PDB entry 1vm8 coloured by chain, side view.
PDB entry 1vm8 coloured by chain, top view.
Source organism: Mus musculus
Entry author: Joint Center for Structural Genomics (JCSG)

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-187612 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylhexosamine pyrophosphorylase Chains: A, B
Molecule details ›
Chains: A, B
Length: 534 amino acids
Theoretical weight: 60.88 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q91YN5 (Residues: 1-522; Coverage: 100%)
Gene name: Uap1
Sequence domains: UTP--glucose-1-phosphate uridylyltransferase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CL 5 x CL
Ligand EDO 2 x EDO
1 modified residue:
Ligand MSE 30 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: P21
Unit cell:
a: 80.094Å b: 73.402Å c: 107.132Å
α: 90° β: 99.83° γ: 90°
R-values:
R R work R free
0.21 0.207 0.266
Expression system: Escherichia coli

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