› 1q6q

X-ray diffraction
1.7Å resolution

Structure of 3-keto-L-gulonate 6-phosphate decarboxylase with bound xylitol 5-phosphate

Released:
DOI: 10.2210/pdb1q6q/pdb
PDB entry 1q6q coloured by chain, front view.
PDB entry 1q6q coloured by chain, side view.
PDB entry 1q6q coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural evidence for a 1,2-enediolate intermediate in the reaction catalyzed by 3-keto-L-gulonate 6-phosphate decarboxylase, a member of the orotidine 5'-monophosphate decarboxylase suprafamily.
Wise EL, Yew WS, Gerlt JA, Rayment I
Biochemistry 42 12133-42 (2003)
PMID: 14567674

Function and Biology Details

Reaction catalysed: 
3-dehydro-L-gulonate 6-phosphate = L-xylulose 5-phosphate + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-153861 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-keto-L-gulonate-6-phosphate decarboxylase UlaD Chains: A, B
Molecule details ›
Chains: A, B
Length: 216 amino acids
Theoretical weight: 23.6 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P39304 (Residues: 1-216; Coverage: 100%)
Gene names: JW4154, b4196, sgaH, ulaD, yjfV
Sequence domains: Orotidine 5'-phosphate decarboxylase / HUMPS family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand LXP 2 x LXP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: C2
Unit cell:
a: 123.182Å b: 41.727Å c: 92.125Å
α: 90° β: 95.87° γ: 90°
R-values:
R R work R free
0.174 0.172 0.207
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Structure of L-xylulose-5-Phosphate 3-epimerase (UlaE) from the anaerobic L-ascorbate utilization pathway of Escherichia coli: identification of a novel phosphate binding motif within a TIM barrel fold.
Shi et al. (2008)
2 more