› 2v3w

X-ray diffraction
2.2Å resolution

Crystal structure of the benzoylformate decarboxylase variant L461A from Pseudomonas putida

Released:
DOI: 10.2210/pdb2v3w/pdb
PDB entry 2v3w coloured by chain, front view.
PDB entry 2v3w coloured by chain, side view.
PDB entry 2v3w coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Rational protein design of ThDP-dependent enzymes-engineering stereoselectivity.
Gocke D, Walter L, Gauchenova E, Kolter G, Knoll M, Berthold CL, Schneider G, Pleiss J, Müller M, Pohl M
Chembiochem 9 406-12 (2008)
PMID: 18224647

Function and Biology Details

Reaction catalysed: 
Benzoylformate = benzaldehyde + CO(2)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149084 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Benzoylformate decarboxylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 528 amino acids
Theoretical weight: 56.36 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P20906 (Residues: 1-528; Coverage: 100%)
Gene name: mdlC
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 4 x TPP
2 bound ligands:
Ligand MG 6 x MG
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: P212121
Unit cell:
a: 95.704Å b: 139.938Å c: 169.054Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.228
Expression system: Escherichia coli

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Citations

2 review citations

Thiamin diphosphate in biological chemistry: exploitation of diverse thiamin diphosphate-dependent enzymes for asymmetric chemoenzymatic synthesis.
Müller et al. (2009)
1 more