› 4lis

X-ray diffraction
2.8Å resolution

Crystal Structure of UDP-galactose-4-epimerase from Aspergillus nidulans

Released:
DOI: 10.2210/pdb4lis/pdb
Model geometry
Fit model/data
PDB entry 4lis coloured by chain, front view.
PDB entry 4lis coloured by chain, side view.
PDB entry 4lis coloured by chain, top view.
Source organism: Aspergillus nidulans FGSC A4
Primary publication:
Elucidation of substrate specificity in Aspergillus nidulans UDP-galactose-4-epimerase.
Dalrymple SA, Ko J, Sheoran I, Kaminskyj SG, Sanders DA
OpenAccess logo PLoS One 8 e76803 (2013)
PMID: 24116166

Function and Biology Details

Reaction catalysed: 
UDP-alpha-D-glucose = UDP-alpha-D-galactose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111801 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-glucose 4-epimerase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 371 amino acids
Theoretical weight: 40.6 KDa
Source organism: Aspergillus nidulans FGSC A4
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: C8VAU8 (Residues: 1-371; Coverage: 100%)
Gene name: ANIA_04727
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 3 x NAD
4 bound ligands:
Ligand UPG 1 x UPG
Ligand GOL 1 x GOL
Ligand IOD 9 x IOD
Ligand UDP 2 x UDP
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: C2
Unit cell:
a: 66.133Å b: 119.154Å c: 161.424Å
α: 90° β: 98.48° γ: 90°
R-values:
R R work R free
0.215 0.213 0.262
Expression system: Escherichia coli BL21

Quick links

Citations

3 citation in other articles

Structural basis for broad substrate specificity of UDP-glucose 4-epimerase in the human milk oligosaccharide catabolic pathway of Bifidobacterium longum.
Nam et al. (2019)
2 more

4 mentions without citation

NADPH oxidase-derived H2O2 subverts pathogen signaling by oxidative phosphotyrosine conversion to PB-DOPA.
Alvarez et al. (2016)
3 more