› 1k0w

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF L-RIBULOSE-5-PHOSPHATE 4-EPIMERASE

Released:
DOI: 10.2210/pdb1k0w/pdb
PDB entry 1k0w coloured by chain, front view.
PDB entry 1k0w coloured by chain, side view.
PDB entry 1k0w coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The structure of L-ribulose-5-phosphate 4-epimerase: an aldolase-like platform for epimerization.
Luo Y, Samuel J, Mosimann SC, Lee JE, Tanner ME, Strynadka NC
Biochemistry 40 14763-71 (2001)
PMID: 11732895

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140030 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ribulose-5-phosphate 4-epimerase AraD Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 231 amino acids
Theoretical weight: 25.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08203 (Residues: 1-231; Coverage: 100%)
Gene names: JW0060, araD, b0061
Sequence domains: Class II Aldolase and Adducin N-terminal domain
Structure domains: Class II aldolase/adducin N-terminal domain

Ligands and Environments

1 bound ligand:
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P4212
Unit cell:
a: 105.9Å b: 105.9Å c: 274.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.251
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Enzymes for the biocatalytic production of rare sugars.
Beerens et al. (2012)
1 more

1 mention without citation

Siamese Network-Based All-Purpose-Tracker, a Model-Free Deep Learning Tool for Animal Behavioral Tracking.
Su et al. (2022)