› 3k8c

X-ray diffraction
2.1Å resolution

Complex of Trypanosoma cruzi ribose 5-phosphate isomerase type B with 4-deoxy-4-phospho-D-erythronohydroxamic acid

Released:
DOI: 10.2210/pdb3k8c/pdb
PDB entry 3k8c coloured by chain, front view.
PDB entry 3k8c coloured by chain, side view.
PDB entry 3k8c coloured by chain, top view.
Source organism: Trypanosoma cruzi strain CL Brener
Primary publication:
Structures of type B ribose 5-phosphate isomerase from Trypanosoma cruzi shed light on the determinants of sugar specificity in the structural family.
Stern AL, Naworyta A, Cazzulo JJ, Mowbray SL
FEBS J 278 793-808 (2011)
PMID: 21205211

Function and Biology Details

Reaction catalysed: 
D-ribose 5-phosphate = D-ribulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-559753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribose 5-phosphate isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 179 amino acids
Theoretical weight: 19.56 KDa
Source organism: Trypanosoma cruzi strain CL Brener
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4CQE2 (Residues: 1-159; Coverage: 100%)
Gene name: Tc00.1047053509199.24
Sequence domains: Ribose/Galactose Isomerase
Structure domains: Sugar-phosphate isomerase, RpiB/LacA/LacB

Ligands and Environments

1 bound ligand:
Ligand RES 2 x RES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P42212
Unit cell:
a: 92.387Å b: 92.387Å c: 94.007Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.217 0.253
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Engineering ribose-5-phosphate isomerase B from a central carbon metabolic enzyme to a promising sugar biocatalyst.
Tang et al. (2021)
1 more

3 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
2 more