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X-ray diffraction
2.5Å resolution

Role of Packing Defects in the Evolution of Allostery and Induced Fit in Human UDP-Glucose Dehydrogenase.

Released:
DOI: 10.2210/pdb3ptz/pdb
PDB entry 3ptz coloured by chain, front view.
PDB entry 3ptz coloured by chain, side view.
PDB entry 3ptz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Role of packing defects in the evolution of allostery and induced fit in human UDP-glucose dehydrogenase.
Kadirvelraj R, Sennett NC, Polizzi SJ, Weitzel S, Wood ZA
Biochemistry 50 5780-9 (2011)
PMID: 21595445

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

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130073 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-glucose 6-dehydrogenase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 494 amino acids
Theoretical weight: 55.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O60701 (Residues: 1-494; Coverage: 100%)
Gene name: UGDH
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 6 x NAD
1 bound ligand:
Ligand UDX 6 x UDX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 89.1Å b: 196.67Å c: 111.744Å
α: 90° β: 111.88° γ: 90°
R-values:
R R work R free
0.192 0.189 0.258
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Packing in molten globules and native states.
Bhattacharyya et al. (2013)
3 more

4 mentions without citation

Allostery and Hysteresis Are Coupled in Human UDP-Glucose Dehydrogenase.
Beattie et al. (2017)
3 more