› 5m49

X-ray diffraction
1.51Å resolution

Alpha-amino epsilon-caprolactam racemase in complex with PLP and D/L alpha amino epsilon-caprolactam (internal aldimine)

Released:
DOI: 10.2210/pdb5m49/pdb
PDB 5m49 coloured by chain and viewed from the front.
PDB 5m49 coloured by chain and viewed from the side.
PDB 5m49 coloured by chain and viewed from the top.
Source organism: Rhizobium freirei PRF 81
Primary publication:
Snapshots of the Catalytic Cycle of the Industrial Enzyme alpha-Amino-epsilon-Caprolactam Racemase (ACLR) Observed Using X-ray Crystallography
Frese A, Sutton PW, Turkenburg JP, Grogan G
ACS Catalysis 7 1045-1048 (2017)

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminotransferase class-III Chain: A
Molecule details ›
Chain: A
Length: 436 amino acids
Theoretical weight: 45.69 KDa
Source organism: Rhizobium freirei PRF 81
Expression system: Escherichia coli
UniProt:
  • Canonical: N6UXY4 (Residues: 1-436; Coverage: 100%)
Gene name: RHSP_08934
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand PLP 1 x PLP
Ligand 8F4 1 x 8F4
Ligand 7F4 1 x 7F4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 87.696Å b: 77.679Å c: 57.602Å
α: 90° β: 112.68° γ: 90°
R-values:
R R work R free
0.163 0.161 0.195
Expression system: Escherichia coli

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