X-ray diffraction
2.6Å resolution

Probing the active site of the sugar isomerase domain from E. coli arabinose-5-phosphate isomerase via X-ray crystallography


Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Arabinose 5-phosphate isomerase KdsD Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 183 amino acids
Theoretical weight: 19.33 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
  • Canonical: P45395 (Residues: 1-183; Coverage: 56%)
Gene names: JW3164, b3197, kdsD, yrbH
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 55.86Å b: 67.43Å c: 82.17Å
α: 90° β: 106.94° γ: 90°
R R work R free
0.263 0.261 0.305
Expression system: Escherichia coli BL21