Entry Database : PDB / ID : 2jf2 Structure visualization Downloads & linksTitle Nucleotide substrate binding by UDP-N-acetylglucosamine acyltransferase ComponentsACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE Details Keywords TRANSFERASE / LIPID A BIOSYNTHESIS / ACYLTRANSFERASE / LIPID SYNTHESISFunction / homology Function and homology informationFunction Domain/homology Component
acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase / acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity / lipid A biosynthetic process / identical protein binding / cytoplasm / cytosol Similarity search - Function Udp N-acetylglucosamine O-acyltransferase; Domain 2 / Udp N-acetylglucosamine O-acyltransferase, C-terminal domain / UDP N-acetylglucosamine O-acyltransferase, C-terminal / UDP-N-acetylglucosamine O-acyltransferase, C-terminal domain superfamily / Udp N-acetylglucosamine O-acyltransferase; Domain 2 / Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase / Hexapeptide transferase, conserved site / Hexapeptide-repeat containing-transferases signature. / Hexapeptide repeat proteins / UDP N-Acetylglucosamine Acyltransferase; domain 1 ... Udp N-acetylglucosamine O-acyltransferase; Domain 2 / Udp N-acetylglucosamine O-acyltransferase, C-terminal domain / UDP N-acetylglucosamine O-acyltransferase, C-terminal / UDP-N-acetylglucosamine O-acyltransferase, C-terminal domain superfamily / Udp N-acetylglucosamine O-acyltransferase; Domain 2 / Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase / 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 / Up-down Bundle / Mainly Beta / Mainly Alpha Similarity search - Domain/homologyBiological species ESCHERICHIA COLI (E. coli)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution : 1.8 Å DetailsAuthors Ulaganathan, V. / Buetow, L. / Hunter, W.N. CitationJournal : J.Mol.Biol. / Year : 2007Title : Nucleotide Substrate Recognition by Udp-N-Acetylglucosamine Acyltransferase (Lpxa) in the First Step of Lipid a Biosynthesis.Authors : Ulaganathan, V. / Buetow, L. / Hunter, W.N. History Deposition Jan 25, 2007 Deposition site : PDBE / Processing site : PDBERevision 1.0 Apr 24, 2007 Provider : repository / Type : Initial releaseRevision 1.1 Dec 4, 2013 Group : Derived calculations / Other ... Derived calculations / Other / Source and taxonomy / Version format compliance Revision 1.2 Dec 13, 2023 Group : Data collection / Database references ... Data collection / Database references / Derived calculations / Other / Refinement description Category : chem_comp_atom / chem_comp_bond ... chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site Item : _database_2.pdbx_DOI / _database_2.pdbx_database_accession ... _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
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