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: 20030408DOI: 10.1021/ja907064w PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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