4N3B

Crystal Structure of human O-GlcNAc Transferase bound to a peptide from HCF-1 pro-repeat2(1-26)E10Q and UDP-5SGlcNAc

Summary for 4N3B

• Entry DOI: 10.2210/pdb4n3b/pdb
• Related: 4N39 4N3A 4N3C
• Descriptor: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, Host cell factor 1, (2S,3R,4R,5S,6R)-3-(acetylamino)-4,5-dihydroxy-6-(hydroxymethyl)tetrahydro-2H-thiopyran-2-yl [(2R,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl dihydrogen diphosphate, ... (4 entities in total)
• Functional Keywords: glycosyltransferase, o-glcnac transferase, proteolysis substrate, tpr domain, tpr binding, transferase-substrate complex, transferase/substrate
• Biological source: Homo sapiens (human); More
• Cellular location: Isoform 2: Mitochondrion. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: O15294; Cytoplasm: P51610
• Total number of polymer chains: 2
• Total formula weight: 84291.80

Authors

Lazarus, M.B.,Herr, W.,Walker, S. (deposition date: 2013-10-06, release date: 2014-01-01, Last modification date: 2024-02-28)

• Primary citation: Lazarus, M.B.,Jiang, J.,Kapuria, V.,Bhuiyan, T.,Janetzko, J.,Zandberg, W.F.,Vocadlo, D.J.,Herr, W.,Walker, S.; HCF-1 is cleaved in the active site of O-GlcNAc transferase.; Science, 342:1235-1239, 2013; PubMed: 24311690; DOI: 10.1126/science.1243990

Experimental method

X-RAY DIFFRACTION (2.17 Å)