5C1D
Human OGT in complex with UDP-5S-GlcNAc and substrate peptide (RB2L)
Summary for 5C1D
Entry DOI | 10.2210/pdb5c1d/pdb |
Descriptor | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit, Retinoblastoma-like protein 2, (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, ... (5 entities in total) |
Functional Keywords | o-glcnac transferase inverting gt-b substrate complex, transferase |
Biological source | Homo sapiens (Human) More |
Cellular location | Isoform 2: Mitochondrion. Isoform 3: Cytoplasm. Isoform 4: Cytoplasm: O15294 Nucleus: Q08999 |
Total number of polymer chains | 2 |
Total formula weight | 82532.70 |
Authors | Schimpl, M.,Rafie, K.,van Aalten, D.M.F. (deposition date: 2015-06-13, 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 Cited by PubMed: 26237509DOI: 10.1038/nsmb.3063 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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