› 1rpx

X-ray diffraction
2.3Å resolution

D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE FROM SOLANUM TUBEROSUM CHLOROPLASTS

Released:
DOI: 10.2210/pdb1rpx/pdb
PDB entry 1rpx coloured by chain, front view.
PDB entry 1rpx coloured by chain, side view.
PDB entry 1rpx coloured by chain, top view.
Source organism: Solanum tuberosum
Primary publication:
Structure and mechanism of the amphibolic enzyme D-ribulose-5-phosphate 3-epimerase from potato chloroplasts.
Kopp J, Kopriva S, Süss KH, Schulz GE
J Mol Biol 287 761-71 (1999)
PMID: 10191144

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174999 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribulose-phosphate 3-epimerase, chloroplastic Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 230 amino acids
Theoretical weight: 24.64 KDa
Source organism: Solanum tuberosum
Expression system: Escherichia coli
UniProt:
  • Canonical: Q43843 (Residues: 47-276; Coverage: 82%)
Sequence domains: Ribulose-phosphate 3 epimerase family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 146.1Å b: 146.1Å c: 93.5Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.174 0.212
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies.
Gerlt et al. (2001)
4 more

5 mentions without citation

Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.
Tabita et al. (2007)
4 more