› 2rjg

X-ray diffraction
2.4Å resolution

Crystal structure of biosynthetic alaine racemase from Escherichia coli

Released:
DOI: 10.2210/pdb2rjg/pdb
PDB entry 2rjg coloured by chain, front view.
PDB entry 2rjg coloured by chain, side view.
PDB entry 2rjg coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: Enzymatic characterization with crystal structure analysis.
Wu D, Hu T, Zhang L, Chen J, Du J, Ding J, Jiang H, Shen X
Protein Sci 17 1066-76 (2008)
PMID: 18434499

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: 379 amino acids
Theoretical weight: 41.42 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21
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
1 bound ligand:
Ligand SO4 12 x SO4
1 modified residue:
Ligand KCX 4 x KCX

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P6
Unit cell:
a: 147.981Å b: 147.981Å c: 163.483Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.214 0.214 0.247
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Exploiting racemases.
Femmer et al. (2016)
18 other articles

5 mentions without citation

Residues Asp164 and Glu165 at the substrate entryway function potently in substrate orientation of alanine racemase from E. coli: Enzymatic characterization with crystal structure analysis.
Wu et al. (2008)
4 more