Entry Database : PDB / ID : 2v0k Structure visualization Downloads & linksTitle Characterization of Substrate Binding and Catalysis of the Potential Antibacterial Target N-acetylglucosamine-1-phosphate Uridyltransferase (GlmU) ComponentsBIFUNCTIONAL PROTEIN GLMU Details Keywords TRANSFERASE / GLMU / CELL WALL / MAGNESIUM / CELL SHAPE / PEPTIDOGLYCAN SYNTHESIS / ASSOCIATIVE MECHANISM / MULTIFUNCTIONAL ENZYME / NUCLEOTIDYLTRANSFERASE / URIDYLATION / METAL-BINDING / ACYLTRANSFERASE / CATALYTIC MECHANISMFunction / homology Function and homology informationFunction Domain/homology Component
glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process / lipid A biosynthetic process / peptidoglycan biosynthetic process / cell morphogenesis / cell wall organization / regulation of cell shape ... glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process / lipid A biosynthetic process / peptidoglycan biosynthetic process / cell morphogenesis / cell wall organization / regulation of cell shape / magnesium ion binding / cytoplasm Similarity search - Function Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase / GlmU, C-terminal LbH domain / MobA-like NTP transferase / MobA-like NTP transferase domain / Hexapeptide transferase, conserved site / Hexapeptide-repeat containing-transferases signature. / Hexapeptide repeat proteins / UDP N-Acetylglucosamine Acyltransferase; domain 1 / Hexapeptide repeat / Bacterial transferase hexapeptide (six repeats) ... Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase / GlmU, C-terminal LbH domain / MobA-like NTP transferase / MobA-like NTP transferase domain / Hexapeptide transferase, conserved site / Hexapeptide-repeat containing-transferases signature. / Hexapeptide repeat proteins / UDP N-Acetylglucosamine Acyltransferase; domain 1 / Hexapeptide repeat / Bacterial transferase hexapeptide (six repeats) / Trimeric LpxA-like superfamily / 3 Solenoid / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A / Nucleotide-diphospho-sugar transferases / Alpha-Beta Complex / Mainly Beta / Alpha Beta Similarity search - Domain/homologyBiological species HAEMOPHILUS INFLUENZAE (bacteria)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 2.3 Å DetailsAuthors Mochalkin, I. / Lightle, S. / Ohren, J.F. / Chirgadze, N.Y. CitationJournal : Protein Sci. / Year : 2007Title : Characterization of Substrate Binding and Catalysis in the Potential Antibacterial Target N-Acetylglucosamine-1-Phosphate Uridyltransferase (Glmu).Authors : Mochalkin, I. / Lightle, S. / Zhu, Y. / Ohren, J.F. / Spessard, C. / Chirgadze, N.Y. / Banotai, C. / Melnick, M. / Mcdowell, L. History Deposition May 14, 2007 Deposition site : PDBE / Processing site : PDBERevision 1.0 Jan 15, 2008 Provider : repository / Type : Initial releaseRevision 1.1 May 8, 2011 Group : Version format complianceRevision 1.2 Jul 13, 2011 Group : Version format complianceRevision 1.3 May 8, 2024 Group : Data collection / Database references / OtherCategory : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Show all Show less Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.