› 4m55

X-ray diffraction
2.86Å resolution

Crystal structure of Human UDP-xylose synthase R236H substitution

Released:
DOI: 10.2210/pdb4m55/pdb
PDB entry 4m55 coloured by chain, front view.
PDB entry 4m55 coloured by chain, side view.
PDB entry 4m55 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Man o' war mutation in UDP-α-D-xylose synthase favors the abortive catalytic cycle and uncovers a latent potential for hexamer formation.
Walsh RM, Polizzi SJ, Kadirvelraj R, Howard WW, Wood ZA
Biochemistry 54 807-19 (2015)
PMID: 25521717

Function and Biology Details

Reaction catalysed: 
UDP-D-glucuronate = UDP-D-xylose + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-185482 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-glucuronic acid decarboxylase 1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 336 amino acids
Theoretical weight: 37.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8NBZ7 (Residues: 85-420; Coverage: 80%)
Gene names: UNQ2538/PRO6079, UXS1
Sequence domains: GDP-mannose 4,6 dehydratase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 6 x NAD
3 bound ligands:
Ligand POP 2 x POP
Ligand SO4 3 x SO4
Ligand UDP 2 x UDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 83.171Å b: 85.145Å c: 292.549Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.231 0.228 0.285
Expression system: Escherichia coli BL21

Quick links

Citations

2 citation in other articles

Mechanistic Insights into Side Effects of Troglitazone and Rosiglitazone Using a Novel Inverse Molecular Docking Protocol.
Kores et al. (2021)
1 more