4MDT
Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine
Summary for 4MDT
Entry DOI | 10.2210/pdb4mdt/pdb |
Descriptor | UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase, ZINC ION, uridine-5'-diphosphate-3-O-(R-3-hydroxymyristoyl)-glucosamine, ... (5 entities in total) |
Functional Keywords | deacetylase, hydrolase |
Biological source | Escherichia coli |
Total number of polymer chains | 4 |
Total formula weight | 139727.43 |
Authors | Clayton, G.M.,Klein, D.J.,Rickert, K.W.,Patel, S.B.,Kornienko, M.,Zugay-Murphy, J.,Reid, J.C.,Tummala, S.,Sharma, S.,Singh, S.B.,Miesel, L.,Lumb, K.J.,Soisson, S.M. (deposition date: 2013-08-23, release date: 2013-10-16, Last modification date: 2023-09-20) |
Primary citation | Clayton, G.M.,Klein, D.J.,Rickert, K.W.,Patel, S.B.,Kornienko, M.,Zugay-Murphy, J.,Reid, J.C.,Tummala, S.,Sharma, S.,Singh, S.B.,Miesel, L.,Lumb, K.J.,Soisson, S.M. Structure of the Bacterial Deacetylase LpxC Bound to the Nucleotide Reaction Product Reveals Mechanisms of Oxyanion Stabilization and Proton Transfer. J.Biol.Chem., 288:34073-34080, 2013 Cited by PubMed: 24108127DOI: 10.1074/jbc.M113.513028 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
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