4UIO

Structure of the Salmonella typhi Type I Dehydroquinase covalently inhibited by a 3-dehydroquinic acid derivative

Summary for 4UIO

Entry DOI	10.2210/pdb4uio/pdb
Descriptor	3-DEHYDROQUINATE DEHYDRATASE, (1~{R},3~{R},4~{S},5~{R})-3-methyl-1,3,4,5-tetrakis(oxidanyl)cyclohexane-1-carboxylic acid, CHLORIDE ION, ... (5 entities in total)
Functional Keywords	bacterial proteins, binding sites, crystallization, lyase, inhibitor, protein binding, shikimis acid pathway, substrate specificity
Biological source	SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHI
Total number of polymer chains	1
Total formula weight	28004.07
Authors	Otero, J.M.,Llamas-Saiz, A.L.,Tizon, L.,Lence, E.,Thompson, P.,Hawkins, A.R.,Gonzalez-Bello, C.,van Raaij, M.J. (deposition date: 2015-03-30, release date: 2015-07-15, Last modification date: 2024-01-10)
Primary citation	Gonzalez-Bello, C.,Tizon, L.,Lence, E.,Otero, J.M.,van Raaij, M.J.,Martinez-Guitian, M.,Beceiro, A.,Thompson, P.,Hawkins, A.R. Chemical Modification of a Dehydratase Enzyme Involved in Bacterial Virulence by an Ammonium Derivative: Evidence of its Active Site Covalent Adduct. J.Am.Chem.Soc., 137:9333-9343, 2015 Cited by PubMed: 26148116 DOI: 10.1021/JACS.5B04080 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.35 Å)

Structure validation