› 1mdl

X-ray diffraction
1.85Å resolution

MANDELATE RACEMASE MUTANT K166R CO-CRYSTALLIZED WITH (R)-MANDELATE

Released:
DOI: 10.2210/pdb1mdl/pdb
PDB entry 1mdl coloured by chain, front view.
PDB entry 1mdl coloured by chain, side view.
PDB entry 1mdl coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Mechanism of the reaction catalyzed by mandelate racemase: structure and mechanistic properties of the K166R mutant.
Kallarakal AT, Mitra B, Kozarich JW, Gerlt JA, Clifton JG, Petsko GA, Kenyon GL
Biochemistry 34 2788-97 (1995)
PMID: 7893690

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: 38.63 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

3 bound ligands:
Ligand MG 1 x MG
Ligand RMN 1 x RMN
Ligand SMN 1 x SMN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I422
Unit cell:
a: 125.32Å b: 125.32Å c: 106.42Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 not available
Expression system: Escherichia coli

Quick links

Citations

5 review citations

"Strong" hydrogen bonds in chemistry and biology.
Perrin et al. (1997)
4 more

3 mentions without citation

Low barrier hydrogen bonds in protein structure and function.
Kemp et al. (2021)
2 more