› 4wr3

X-ray diffraction
1.9Å resolution

Y274F alanine racemase from E. coli

Released:
DOI: 10.2210/pdb4wr3/pdb
PDB entry 4wr3 coloured by chain, front view.
PDB entry 4wr3 coloured by chain, side view.
PDB entry 4wr3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Mechanistic and Evolutionary Insights from the Reciprocal Promiscuity of Two Pyridoxal Phosphate-dependent Enzymes.
Soo VW, Yosaatmadja Y, Squire CJ, Patrick WM
J Biol Chem 291 19873-87 (2016)
PMID: 27474741

Function and Biology Details

Reaction catalysed: 
L-alanine = D-alanine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141289 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alanine racemase, biosynthetic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 359 amino acids
Theoretical weight: 39.19 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6B4 (Residues: 1-359; Coverage: 100%)
Gene names: JW4013, alr, b4053
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
2 bound ligands:
Ligand SO4 5 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P6
Unit cell:
a: 148.079Å b: 148.079Å c: 163.689Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.175 0.204
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Review: Engineering of thermostable enzymes for industrial applications.
Rigoldi et al. (2018)
3 more

3 mentions without citation

Mechanistic and Evolutionary Insights from the Reciprocal Promiscuity of Two Pyridoxal Phosphate-dependent Enzymes.
Soo et al. (2016)
2 more