3IAF

Structure of benzaldehyde lyase A28S mutant with monomethyl benzoylphosphonate

Summary for 3IAF

Entry DOI	10.2210/pdb3iaf/pdb
Related	3IAE
Descriptor	Benzaldehyde lyase, THIAMINE DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
Functional Keywords	phosphoserine, covalent sidechain adduct, lyase
Biological source	Pseudomonas fluorescens
Total number of polymer chains	4
Total formula weight	241694.60
Authors	Brandt, G.S.,Petsko, G.A.,Ringe, D.,McLeish, M.J. (deposition date: 2009-07-13, release date: 2010-03-02, Last modification date: 2023-09-06)
Primary citation	Brandt, G.S.,Kneen, M.M.,Petsko, G.A.,Ringe, D.,McLeish, M.J. Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition. J.Am.Chem.Soc., 132:438-439, 2010 Cited by PubMed: 20030408 DOI: 10.1021/ja907064w PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.8 Å)

Structure validation