› 5ll2

X-ray diffraction
2.6Å resolution

Structure of Isoleucine 2-epimerase from Lactobacillus buchneri (apo form)

Released:
DOI: 10.2210/pdb5ll2/pdb
Model geometry
Fit model/data
PDB entry 5ll2 coloured by chain, front view.
PDB entry 5ll2 coloured by chain, side view.
PDB entry 5ll2 coloured by chain, top view.
Source organism: Lentilactobacillus buchneri
Primary publication:
Structural insights into the substrate recognition and reaction specificity of the PLP-dependent fold-type I isoleucine 2-epimerase from Lactobacillus buchneri.
Awad R, Gans P, Reiser JB
Biochimie 137 165-173 (2017)
PMID: 28344038

Function and Biology Details

Reaction catalysed: 
L-isoleucine = D-allo-isoleucine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125924 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoleucine 2-epimerase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 480 amino acids
Theoretical weight: 52.85 KDa
Source organism: Lentilactobacillus buchneri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: M1GRN3 (Residues: 1-450; Coverage: 100%)
Sequence domains: Aminotransferase class-III
Structure domains: Type I PLP-dependent aspartate aminotransferase-like (Major domain)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE MASSIF-3
Spacegroup: P212121
Unit cell:
a: 59.16Å b: 161.78Å c: 186.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.244 0.316
Expression system: Escherichia coli BL21(DE3)

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Citations

1 citations in other articles

Structural and functional insight into serine hydroxymethyltransferase from Helicobacter pylori.
Sodolescu et al. (2018)