› 3iaf

X-ray diffraction
2.8Å resolution

Structure of benzaldehyde lyase A28S mutant with monomethyl benzoylphosphonate

Released:
DOI: 10.2210/pdb3iaf/pdb
PDB entry 3iaf coloured by chain, front view.
PDB entry 3iaf coloured by chain, side view.
PDB entry 3iaf coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition.
Brandt GS, Kneen MM, Petsko GA, Ringe D, McLeish MJ
J Am Chem Soc 132 438-9 (2010)
PMID: 20030408

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: 570 amino acids
Theoretical weight: 59.97 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9F4L3 (Residues: 1-562; 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
1 modified residue:
Ligand SEP 4 x SEP

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3121
Unit cell:
a: 150.962Å b: 150.962Å c: 195.56Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.213 0.26
Expression system: Escherichia coli

Quick links

Citations

2 review citations

CC bond formation using ThDP-dependent lyases.
Müller et al. (2013)
1 more

1 mention without citation

Forcefield_PTM: Ab Initio Charge and AMBER Forcefield Parameters for Frequently Occurring Post-Translational Modifications.
Khoury et al. (2013)