› 3int

X-ray diffraction
2.51Å resolution

Structure of UDP-galactopyranose mutase bound to UDP-galactose (reduced)

Released:
DOI: 10.2210/pdb3int/pdb
PDB entry 3int coloured by chain, front view.
PDB entry 3int coloured by chain, side view.
PDB entry 3int coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
X-ray crystallography reveals a reduced substrate complex of UDP-galactopyranose mutase poised for covalent catalysis by flavin.
Gruber TD, Westler WM, Kiessling LL, Forest KT
Biochemistry 48 9171-3 (2009)
PMID: 19719175

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-175360 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-galactopyranose mutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 45.24 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q48485 (Residues: 1-384; Coverage: 100%)
Gene name: rfbD
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand FDA 2 x FDA
2 bound ligands:
Ligand UDP 1 x UDP
Ligand GDU 1 x GDU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P41
Unit cell:
a: 94.078Å b: 94.078Å c: 129.443Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.247
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Flavoenzymes: versatile catalysts in biosynthetic pathways.
Walsh et al. (2013)
3 more

11 mentions without citation

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