› 6c4k

X-ray diffraction
2.65Å resolution

Full length hUGDH with A104L substitution in the absence of ligand

Released:
DOI: 10.2210/pdb6c4k/pdb
PDB entry 6c4k coloured by chain, front view.
PDB entry 6c4k coloured by chain, side view.
PDB entry 6c4k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Hysteresis and Allostery in Human UDP-Glucose Dehydrogenase Require a Flexible Protein Core.
Beattie NR, Pioso BJ, Sidlo AM, Keul ND, Wood ZA
Biochemistry 57 6848-6859 (2018)
PMID: 30457329

Function and Biology Details

Reaction catalysed: 
UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-130072 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-glucose 6-dehydrogenase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 494 amino acids
Theoretical weight: 55.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60701 (Residues: 1-494; Coverage: 100%)
Gene name: UGDH
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand PO4 3 x PO4
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 178.52Å b: 114.47Å c: 96.88Å
α: 90° β: 116.5° γ: 90°
R-values:
R R work R free
0.223 0.222 0.255
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Conservation of Atypical Allostery in C. elegans UDP-Glucose Dehydrogenase.
Beattie et al. (2019)
1 more

1 mention without citation

Hysteresis and Allostery in Human UDP-Glucose Dehydrogenase Require a Flexible Protein Core.
Beattie et al. (2018)