› 3dxw

X-ray diffraction
2.41Å resolution

The crystal structure of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae complexed with epsilon caprolactam

Released:
DOI: 10.2210/pdb3dxw/pdb
PDB entry 3dxw coloured by chain, front view.
PDB entry 3dxw coloured by chain, side view.
PDB entry 3dxw coloured by chain, top view.
Source organism: Achromobacter obae
Primary publication:
The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae.
Okazaki S, Suzuki A, Mizushima T, Kawano T, Komeda H, Asano Y, Yamane T
Biochemistry 48 941-50 (2009)
PMID: 19146406

Function and Biology Details

Reaction catalysed: 
(S)-2-aminohexano-6-lactam = (R)-2-aminohexano-6-lactam
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181691 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-aminohexano-6-lactam racemase Chains: A, B
Molecule details ›
Chains: A, B
Length: 452 amino acids
Theoretical weight: 47.56 KDa
Source organism: Achromobacter obae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7M181 (Residues: 1-436; Coverage: 100%)
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
1 bound ligand:
Ligand ICC 2 x ICC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P21
Unit cell:
a: 56.581Å b: 60.653Å c: 105.315Å
α: 90° β: 103.07° γ: 90°
R-values:
R R work R free
0.194 0.191 0.252
Expression system: Escherichia coli

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Citations

2 review citations

Bioinformatic analysis of a PLP-dependent enzyme superfamily suitable for biocatalytic applications.
Steffen-Munsberg et al. (2015)
1 more