› 3ovq

X-ray diffraction
2Å resolution

Crystal Structure of hRPE and D-Ribulose-5-Phospate Complex

Released:
DOI: 10.2210/pdb3ovq/pdb
PDB entry 3ovq coloured by chain, front view.
PDB entry 3ovq coloured by chain, side view.
PDB entry 3ovq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE.
Liang W, Ouyang S, Shaw N, Joachimiak A, Zhang R, Liu ZJ
FASEB J 25 497-504 (2011)
PMID: 20923965

Function and Biology Details

Reaction catalysed: 
D-ribulose 5-phosphate = D-xylulose 5-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188362 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribulose-phosphate 3-epimerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 228 amino acids
Theoretical weight: 24.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96AT9 (Residues: 1-228; Coverage: 100%)
Gene names: HUSSY-17, RPE
Sequence domains: Ribulose-phosphate 3 epimerase family
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand FE2 2 x FE2
Ligand 5RP 2 x 5RP
Ligand XPE 7 x XPE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21
Unit cell:
a: 61.785Å b: 43.535Å c: 72.269Å
α: 90° β: 94.88° γ: 90°
R-values:
R R work R free
0.15 0.147 0.191
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Effects of Metabolism on Macrophage Polarization Under Different Disease Backgrounds.
Sun et al. (2022)
2 more

4 mentions without citation

Conversion of D-ribulose 5-phosphate to D-xylulose 5-phosphate: new insights from structural and biochemical studies on human RPE.
Liang et al. (2011)
3 more