4KGD

High-resolution crystal structure of pyruvate oxidase from L. plantarum in complex with phosphate

Summary for 4KGD

Entry DOI	10.2210/pdb4kgd/pdb
Related	4FEE
Descriptor	Pyruvate oxidase, FLAVIN-ADENINE DINUCLEOTIDE, MAGNESIUM ION, ... (8 entities in total)
Functional Keywords	carbanion, structure activity relationship, oxidation-reduction, umpolung, thiamine diphosphate, reaction intermediate, oxidoreductase
Biological source	Lactobacillus plantarum
Total number of polymer chains	2
Total formula weight	135941.82
Authors	Neumann, P.,Tittmann, K. (deposition date: 2013-04-29, release date: 2013-06-12, Last modification date: 2023-09-20)
Primary citation	Meyer, D.,Neumann, P.,Ficner, R.,Tittmann, K. Observation of a stable carbene at the active site of a thiamin enzyme. Nat.Chem.Biol., 9:488-490, 2013 Cited by PubMed Abstract: Carbenes are highly reactive chemical compounds that are exploited as ligands in organometallic chemistry and are powerful organic catalysts. They were postulated to occur as transient intermediates in enzymes, yet their existence in a biological system could never be demonstrated directly. We present spectroscopic and structural data of a thiamin enzyme in a noncovalent complex with substrate, which implicate accumulation of a stable carbene as a major resonance contributor to deprotonated thiamin. PubMed: 23748673 DOI: 10.1038/nchembio.1275 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.06 Å)

Structure validation