› 2ag0

X-ray diffraction
2.58Å resolution

Crystal structure of Benzaldehyde lyase (BAL)- native

Released:
DOI: 10.2210/pdb2ag0/pdb
PDB entry 2ag0 coloured by chain, front view.
PDB entry 2ag0 coloured by chain, side view.
PDB entry 2ag0 coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens.
Mosbacher TG, Mueller M, Schulz GE
FEBS J 272 6067-76 (2005)
PMID: 16302970

Function and Biology Details

Reaction catalysed: 
Benzoin = 2 benzaldehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190253 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Benzaldehyde lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 563 amino acids
Theoretical weight: 58.98 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F4L3 (Residues: 1-563; Coverage: 100%)
Gene name: bznB
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand TPP 4 x TPP
1 bound ligand:
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P3121
Unit cell:
a: 154.72Å b: 154.72Å c: 200.7Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.2 0.22
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

6 mentions without citation

Computational protein design enables a novel one-carbon assimilation pathway.
Siegel et al. (2015)
5 more