› 4u8m

X-ray diffraction
2.3Å resolution

Structure of Aspergillus fumigatus UDP-Galactopyranose mutase mutant Y317A

Released:
DOI: 10.2210/pdb4u8m/pdb
PDB entry 4u8m coloured by chain, front view.
PDB entry 4u8m coloured by chain, side view.
PDB entry 4u8m coloured by chain, top view.
Source organism: Aspergillus fumigatus
Primary publication:
Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics.
Da Fonseca I, Qureshi IA, Mehra-Chaudhary R, Kizjakina K, Tanner JJ, Sobrado P
Biochemistry 53 7794-804 (2014)
PMID: 25412209

Function and Biology Details

Reaction catalysed: 
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175786 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-galactopyranose mutase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 513 amino acids
Theoretical weight: 57.04 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4W1X2 (Residues: 1-510; Coverage: 100%)
Gene names: glf, glfA
Sequence domains: NAD(P)-binding Rossmann-like domain
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FDA 4 x FDA
2 bound ligands:
Ligand SO4 23 x SO4
Ligand EDO 17 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P6522
Unit cell:
a: 216.564Å b: 216.564Å c: 317.291Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.206 0.204 0.244
Expression system: Escherichia coli

Quick links

Citations

1 review citation

N5 Is the New C4a: Biochemical Functionalization of Reduced Flavins at the N5 Position.
Beaupre et al. (2020)
4 other articles

1 mention without citation

Contributions of unique active site residues of eukaryotic UDP-galactopyranose mutases to substrate recognition and active site dynamics.
Da Fonseca et al. (2014)