2QIV
Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase
Summary for 2QIV
Entry DOI | 10.2210/pdb2qiv/pdb |
Related | 2QIA |
Descriptor | UDP-N-acetylglucosamine acyltransferase, uridine-5'-diphosphate-3-O-(R-3-hydroxydecanoyl)-N-acetyl-D-glucosamine (3 entities in total) |
Functional Keywords | left-handed parallel beta helix; protein lipid recognition, transferase |
Biological source | Escherichia coli K12 |
Cellular location | Cytoplasm: P0A722 |
Total number of polymer chains | 1 |
Total formula weight | 28894.62 |
Authors | Williams, A.H.,Raetz, C.R.H. (deposition date: 2007-07-05, release date: 2007-10-02, Last modification date: 2024-02-21) |
Primary citation | Williams, A.H.,Raetz, C.R.H. Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase Proc.Natl.Acad.Sci.Usa, 104:13543-13550, 2007 Cited by PubMed: 17698807DOI: 10.1073/pnas.0705833104 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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