› 1a9z

X-ray diffraction
1.9Å resolution

UDP-GALACTOSE 4-EPIMERASE MUTANT S124A/Y149F COMPLEXED WITH UDP-GALACTOSE

Released:
DOI: 10.2210/pdb1a9z/pdb
PDB entry 1a9z coloured by chain, front view.
PDB entry 1a9z coloured by chain, side view.
PDB entry 1a9z coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli.
Thoden JB, Holden HM
Biochemistry 37 11469-77 (1998)
PMID: 9708982

Function and Biology Details

Reaction catalysed: 
UDP-alpha-D-glucose = UDP-alpha-D-galactose
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-140567 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-glucose 4-epimerase Chain: A
Molecule details ›
Chain: A
Length: 338 amino acids
Theoretical weight: 37.26 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P09147 (Residues: 1-338; Coverage: 100%)
Gene names: JW0742, b0759, galD, galE
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 1 x NAD
3 bound ligands:
Ligand NA 3 x NA
Ligand UPG 1 x UPG
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P3221
Unit cell:
a: 83.9Å b: 83.9Å c: 108.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.188 not available
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Structure and function of enzymes of the Leloir pathway for galactose metabolism.
Holden et al. (2003)
5 more

4 mentions without citation

Functional characterization of Gne (UDP-N-acetylglucosamine-4-epimerase), Wzz (chain length determinant), and Wzy (O-antigen polymerase) of Yersinia enterocolitica serotype O:8.
Bengoechea et al. (2002)
3 more