4GZ6
Crystal structure of human O-GlcNAc Transferase with UDP-5SGlcNAc
Summary for 4GZ6
Entry DOI | 10.2210/pdb4gz6/pdb |
Related | 4GYW 4GYY 4GZ3 4GZ5 |
Descriptor | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, (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, SULFATE ION, ... (4 entities in total) |
Functional Keywords | ogt, o-glcnac, gt-b, glycosyltransferase, o-glcnacylation, transferase |
Biological source | Homo sapiens (human) |
Cellular location | Isoform 2: Mitochondrion. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: O15294 |
Total number of polymer chains | 4 |
Total formula weight | 328024.78 |
Authors | Lazarus, M.B.,Jiang, J.,Gloster, T.M.,Zandberg, W.F.,Vocadlo, D.J.,Walker, S. (deposition date: 2012-09-06, release date: 2012-10-31, Last modification date: 2024-02-28) |
Primary citation | Lazarus, M.B.,Jiang, J.,Gloster, T.M.,Zandberg, W.F.,Whitworth, G.E.,Vocadlo, D.J.,Walker, S. Structural snapshots of the reaction coordinate for O-GlcNAc transferase. Nat.Chem.Biol., 8:966-968, 2012 Cited by PubMed Abstract: Visualization of the reaction coordinate undertaken by glycosyltransferases has remained elusive but is critical for understanding this important class of enzyme. Using substrates and substrate mimics, we describe structural snapshots of all species along the kinetic pathway for human O-linked β-N-acetylglucosamine transferase (O-GlcNAc transferase), an intracellular enzyme that catalyzes installation of a dynamic post-translational modification. The structures reveal key features of the mechanism and show that substrate participation is important during catalysis. PubMed: 23103939DOI: 10.1038/nchembio.1109 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.98 Å) |
Structure validation
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