› 3gf4

X-ray diffraction
2.45Å resolution

Structure of UDP-galactopyranose mutase bound to UDP-glucose

Released:
DOI: 10.2210/pdb3gf4/pdb
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Source organism: Klebsiella pneumoniae
Primary publication:
Ligand binding and substrate discrimination by UDP-galactopyranose mutase.
Gruber TD, Borrok MJ, Westler WM, Forest KT, Kiessling LL
J Mol Biol 391 327-40 (2009)
PMID: 19500588

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 FAD 2 x FAD
2 bound ligands:
Ligand UPG 1 x UPG
Ligand U5P 1 x U5P
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 14-ID-B
Spacegroup: P41
Unit cell:
a: 93.951Å b: 93.951Å c: 130.259Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.238
Expression system: Escherichia coli

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Citations

2 review citations

Bioinformatics and Drug Discovery.
Xia X. (2017)
1 more

7 mentions without citation

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

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