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4MDT

Structure of LpxC bound to the reaction product UDP-(3-O-(R-3-hydroxymyristoyl))-glucosamine

Summary for 4MDT
Entry DOI10.2210/pdb4mdt/pdb
DescriptorUDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase, ZINC ION, uridine-5'-diphosphate-3-O-(R-3-hydroxymyristoyl)-glucosamine, ... (5 entities in total)
Functional Keywordsdeacetylase, hydrolase
Biological sourceEscherichia coli
Total number of polymer chains4
Total formula weight139727.43
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 citationClayton, 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: 24108127
DOI: 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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