› 4a6g

X-ray diffraction
2.71Å resolution

N-acyl amino acid racemase from Amycalotopsis sp. Ts-1-60: G291D- F323Y mutant in complex with N-acetyl methionine

Released:
DOI: 10.2210/pdb4a6g/pdb
PDB entry 4a6g coloured by chain, front view.
PDB entry 4a6g coloured by chain, side view.
PDB entry 4a6g coloured by chain, top view.
Source organism: Amycolatopsis sp.
Primary publication:
An improved racemase/acylase biotransformation for the preparation of enantiomerically pure amino acids.
Baxter S, Royer S, Grogan G, Brown F, Holt-Tiffin KE, Taylor IN, Fotheringham IG, Campopiano DJ
J Am Chem Soc 134 19310-3 (2012)
PMID: 23130969

Function and Biology Details

Reaction catalysed: 
(1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate = 2-succinylbenzoate + H(2)O
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-175017 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-succinylamino acid racemase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 368 amino acids
Theoretical weight: 39.52 KDa
Source organism: Amycolatopsis sp.
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q44244 (Residues: 1-368; Coverage: 100%)
Gene name: Aaar
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand AME 4 x AME
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: R32
Unit cell:
a: 216.71Å b: 216.71Å c: 261.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.155 0.21
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Enzymes from Extreme Environments and Their Industrial Applications.
Littlechild JA. (2015)
4 more

1 mention without citation

Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.
Lloyd et al. (2021)