› 3ukq

X-ray diffraction
3.15Å resolution

Crystal structure of R327K UDP-galactopyranose mutase from Aspergillus fumigatus in complex with UDPgalp

Released:
DOI: 10.2210/pdb3ukq/pdb
PDB entry 3ukq coloured by chain, front view.
PDB entry 3ukq coloured by chain, side view.
PDB entry 3ukq coloured by chain, top view.
Source organism: Aspergillus fumigatus
Primary publication:
Structural insight into the unique substrate binding mechanism and flavin redox state of UDP-galactopyranose mutase from Aspergillus fumigatus.
van Straaten KE, Routier FH, Sanders DA
J Biol Chem 287 10780-90 (2012)
PMID: 22334662

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: 510 amino acids
Theoretical weight: 56.91 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4W1X2 (Residues: 2-510; 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 FAD 4 x FAD
1 bound ligand:
Ligand GDU 4 x GDU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08B1-1
Spacegroup: P212121
Unit cell:
a: 129.54Å b: 135.48Å c: 176.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.248
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Targeting UDP-galactopyranose mutases from eukaryotic human pathogens.
Kizjakina et al. (2013)
3 more

3 mentions without citation

Structure, mechanism, and dynamics of UDP-galactopyranose mutase.
Tanner et al. (2014)
2 more