› 1ek6

X-ray diffraction
1.5Å resolution

STRUCTURE OF HUMAN UDP-GALACTOSE 4-EPIMERASE COMPLEXED WITH NADH AND UDP-GLUCOSE

Released:
DOI: 10.2210/pdb1ek6/pdb
PDB entry 1ek6 coloured by chain, front view.
PDB entry 1ek6 coloured by chain, side view.
PDB entry 1ek6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystallographic evidence for Tyr 157 functioning as the active site base in human UDP-galactose 4-epimerase.
Thoden JB, Wohlers TM, Fridovich-Keil JL, Holden HM
Biochemistry 39 5691-701 (2000)
PMID: 10801319

Function and Biology Details

Reactions catalysed: 
UDP-alpha-D-glucose = UDP-alpha-D-galactose
UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-galactosamine
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-171995 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-glucose 4-epimerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 348 amino acids
Theoretical weight: 38.32 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: Q14376 (Residues: 1-348; Coverage: 100%)
Gene name: GALE
Sequence domains: GDP-mannose 4,6 dehydratase
Structure domains:

Ligands and Environments


Cofactor: Ligand NAI 2 x NAI
3 bound ligands:
Ligand MG 2 x MG
Ligand UPG 2 x UPG
Ligand TMA 3 x TMA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 74.7Å b: 86.9Å c: 95.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.198
Expression system: Saccharomyces cerevisiae

Quick links

Citations

11 review citations

Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes.
Kavanagh et al. (2008)
10 more

20 mentions without citation

Low barrier hydrogen bonds in protein structure and function.
Kemp et al. (2021)
19 more