› 3he3

X-ray diffraction
2.4Å resolution

Crystal Structure of UDP-galactopyranose mutase in complex with UDP

Released:
DOI: 10.2210/pdb3he3/pdb
PDB entry 3he3 coloured by chain, front view.
PDB entry 3he3 coloured by chain, side view.
PDB entry 3he3 coloured by chain, top view.
Source organism: Deinococcus radiodurans
Primary publication:
Structural basis of substrate binding to UDP-galactopyranose mutase: crystal structures in the reduced and oxidized state complexed with UDP-galactopyranose and UDP.
Partha SK, van Straaten KE, Sanders DA
J Mol Biol 394 864-77 (2009)
PMID: 19836401

Function and Biology Details

Reaction catalysed: 
UDP-alpha-D-galactopyranose = UDP-alpha-D-galactofuranose
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo decamer
Assembly name:
PDBe Complex ID:
PDB-CPX-193354 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-galactopyranose mutase C-terminal domain-containing protein Chains: A, B, C, D, E, F, G, H, I, J
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J
Length: 397 amino acids
Theoretical weight: 45.74 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RYF1 (Residues: 1-397; Coverage: 100%)
Gene name: DR_A0367
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand FAD 10 x FAD
1 bound ligand:
Ligand UDP 10 x UDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 134.05Å b: 176.874Å c: 222.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.254
Expression system: Escherichia coli

Quick links

Citations

5 review citations

The structural biology of enzymes involved in natural product glycosylation.
Singh et al. (2012)
4 more

4 mentions without citation

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