› 1lrl

X-ray diffraction
1.8Å resolution

Crystal Structure of UDP-Galactose 4-Epimerase Mutant Y299C Complexed with UDP-Glucose

Released:
DOI: 10.2210/pdb1lrl/pdb
PDB entry 1lrl coloured by chain, front view.
PDB entry 1lrl coloured by chain, side view.
PDB entry 1lrl coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural analysis of the Y299C mutant of Escherichia coli UDP-galactose 4-epimerase. Teaching an old dog new tricks.
Thoden JB, Henderson JM, Fridovich-Keil JL, Holden HM
J Biol Chem 277 27528-34 (2002)
PMID: 12019271

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: 37.23 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 2 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 RU200
Spacegroup: P3221
Unit cell:
a: 83.2Å b: 83.2Å c: 109.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.194 0.261
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Predicting protein function from structure--the roles of short-chain dehydrogenase/reductase enzymes in Bordetella O-antigen biosynthesis.
King et al. (2007)
1 more