› 1de6

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
L-rhamnopyranose = L-rhamnulose
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-152219 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-rhamnose isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 426 amino acids
Theoretical weight: 48.17 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P32170 (Residues: 1-419; Coverage: 100%)
Gene names: JW5561, b3903, rhaA
Sequence domains: L-rhamnose isomerase (RhaA)
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

3 bound ligands:
Ligand RNS 4 x RNS
Ligand ZN 4 x ZN
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 169.179Å b: 162.439Å c: 77.726Å
α: 90° β: 109.89° γ: 90°
R-values:
R R work R free
0.177 0.244 0.244
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Isomerases for biotransformation of D-hexoses.
Mu et al. (2015)
1 more

3 mentions without citation

Evolution of the arginase fold and functional diversity.
Dowling et al. (2008)
2 more