2XMZ

Structure of MenH from S. aureus

Summary for 2XMZ

Entry DOI	10.2210/pdb2xmz/pdb
Descriptor	HYDROLASE, ALPHA/BETA HYDROLASE FOLD FAMILY (2 entities in total)
Functional Keywords	menaquinone biosynthesis, lyase
Biological source	STAPHYLOCOCCUS AUREUS
Total number of polymer chains	1
Total formula weight	31019.18
Authors	Dawson, A.,Fyfe, P.K.,Gillet, F.,Hunter, W.N. (deposition date: 2010-07-30, release date: 2011-05-25, Last modification date: 2023-12-20)
Primary citation	Dawson, A.,Fyfe, P.K.,Gillet, F.,Hunter, W.N. Exploiting the High-Resolution Crystal Structure of Staphylococcus Aureus Menh to Gain Insight Into Enzyme Activity. Bmc Struct.Biol., 11:19-, 2011 Cited by PubMed Abstract: MenH (2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase) is a key enzyme in the biosynthesis of menaquinone, catalyzing an unusual 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate. PubMed: 21513522 DOI: 10.1186/1472-6807-11-19 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.94 Å)

Structure validation