› 1lk7

X-ray diffraction
2Å resolution

Structure of D-Ribose-5-Phosphate Isomerase from in complex with phospho-erythronic acid

Released:
DOI: 10.2210/pdb1lk7/pdb
PDB entry 1lk7 coloured by chain, front view.
PDB entry 1lk7 coloured by chain, side view.
PDB entry 1lk7 coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure.
Ishikawa K, Matsui I, Payan F, Cambillau C, Ishida H, Kawarabayasi Y, Kikuchi H, Roussel A
Structure 10 877-86 (2002)
PMID: 12057201

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribose-5-phosphate isomerase A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 229 amino acids
Theoretical weight: 25.19 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O50083 (Residues: 1-229; Coverage: 100%)
Gene names: PH1375, rpiA
Sequence domains: Ribose 5-phosphate isomerase A (phosphoriboisomerase A)
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CL 10 x CL
Ligand NA 2 x NA
Ligand DER 4 x DER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 73.689Å b: 114.923Å c: 119.578Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.247
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Role of Na+ and K+ in enzyme function.
Page et al. (2006)
3 more

3 mentions without citation

A Bacterial Pathogen Senses Host Mannose to Coordinate Virulence.
Wei et al. (2019)
2 more