3p14

X-ray diffraction
2.51Å resolution

Crystal structure of L-rhamnose isomerase with a novel high thermo-stability from Bacillus halodurans

Released:

Function and Biology Details

Reaction catalysed:
L-rhamnopyranose = L-rhamnulose
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191832 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-rhamnose isomerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 424 amino acids
Theoretical weight: 49.08 KDa
Source organism: Alkalihalobacillus halodurans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KCL9 (Residues: 1-418; Coverage: 100%)
Gene names: BH1552, rhaA
Sequence domains: L-rhamnose isomerase (RhaA)
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6C1
Spacegroup: P21
Unit cell:
a: 83.24Å b: 164.88Å c: 92.01Å
α: 90° β: 115.97° γ: 90°
R-values:
R R work R free
0.189 0.185 0.256
Expression system: Escherichia coli