› 1dtn

X-ray diffraction
2.1Å resolution

MANDELATE RACEMASE MUTANT D270N CO-CRYSTALLIZED WITH (S)-ATROLACTATE

Released:
DOI: 10.2210/pdb1dtn/pdb
PDB entry 1dtn coloured by chain, front view.
PDB entry 1dtn coloured by chain, side view.
PDB entry 1dtn coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Mechanism of the reaction catalyzed by mandelate racemase: importance of electrophilic catalysis by glutamic acid 317.
Mitra B, Kallarakal AT, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL
Biochemistry 34 2777-87 (1995)
PMID: 7893689

Function and Biology Details

Reaction catalysed: 
(S)-mandelate = (R)-mandelate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145839 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mandelate racemase Chain: A
Molecule details ›
Chain: A
Length: 359 amino acids
Theoretical weight: 38.6 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: P11444 (Residues: 1-359; Coverage: 100%)
Gene name: mdlA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand APG 1 x APG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I422
Unit cell:
a: 125.5Å b: 125.5Å c: 107.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 not available
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity.
Gerlt et al. (2005)
4 more

1 mention without citation

Insights into the fold organization of TIM barrel from interaction energy based structure networks.
Vijayabaskar et al. (2012)