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: 26148116DOI: 10.1021/JACS.5B04080 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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