› 4fp1

X-ray diffraction
1.68Å resolution

P. putida mandelate racemase co-crystallized with 3,3,3-trifluoro-2-hydroxy-2-(trifluoromethyl) propionic acid

Released:
DOI: 10.2210/pdb4fp1/pdb
PDB entry 4fp1 coloured by chain, front view.
PDB entry 4fp1 coloured by chain, side view.
PDB entry 4fp1 coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Potent inhibition of mandelate racemase by a fluorinated substrate-product analogue with a novel binding mode.
Nagar M, Lietzan AD, St Maurice M, Bearne SL
Biochemistry 53 1169-78 (2014)
PMID: 24472022

Function and Biology Details

Reaction catalysed: 
(S)-mandelate = (R)-mandelate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence 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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 383 amino acids
Theoretical weight: 41.3 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11444 (Residues: 1-359; Coverage: 100%)
Gene name: mdlA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand BFM 2 x BFM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: I422
Unit cell:
a: 148.87Å b: 148.87Å c: 169.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.193
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

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

1 mention without citation

Capturing the free energy of transition state stabilization: insights from the inhibition of mandelate racemase.
Bearne SL. (2023)