5BNW

The active site of O-GlcNAc transferase imposes constraints on substrate sequence

Summary for 5BNW

• Entry DOI: 10.2210/pdb5bnw/pdb
• Descriptor: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, laminB1 residues 179-191, (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: o-glcnac transferase, glycosyl transferase, transferase
• Biological source: Homo sapiens (Human); More
• Cellular location: Isoform 2: Mitochondrion. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: O15294
• Total number of polymer chains: 2
• Total formula weight: 82944.46

Authors

Pathak, S.,Alonso, J.,Schimpl, M.,Rafie, K.,Blair, D.E.,Borodkin, V.S.,Albarbarawi, O.,van Aalten, D.M.F. (deposition date: 2015-05-26, release date: 2015-08-05, Last modification date: 2024-01-10)

• Primary citation: Pathak, S.,Alonso, J.,Schimpl, M.,Rafie, K.,Blair, D.E.,Borodkin, V.S.,Schuttelkopf, A.W.,Albarbarawi, O.,van Aalten, D.M.; The active site of O-GlcNAc transferase imposes constraints on substrate sequence.; Nat.Struct.Mol.Biol., 22:744-750, 2015; PubMed: 26237509; DOI: 10.1038/nsmb.3063

Experimental method

X-RAY DIFFRACTION (2.4 Å)