› 4x2p

X-ray diffraction
1.65Å resolution

P. putida mandelate racemase in complex with 3-hydroxypyruvate

Released:
DOI: 10.2210/pdb4x2p/pdb
PDB entry 4x2p coloured by chain, front view.
PDB entry 4x2p coloured by chain, side view.
PDB entry 4x2p coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Inactivation of Mandelate Racemase by 3-Hydroxypyruvate Reveals a Potential Mechanistic Link between Enzyme Superfamilies.
Nagar M, Wyatt BN, St Maurice M, Bearne SL
Biochemistry 54 2747-57 (2015)
PMID: 25844917

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 Chain: A
Molecule details ›
Chain: A
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 3PY 1 x 3PY
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: I422
Unit cell:
a: 123.879Å b: 123.879Å c: 105.301Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.145 0.143 0.177
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)

1 mention without citation

Self-association of a highly charged arginine-rich cell-penetrating peptide.
Tesei et al. (2017)