5M7T
Structure of human O-GlcNAc hydrolase with PugNAc type inhibitor
Summary for 5M7T
| Entry DOI | 10.2210/pdb5m7t/pdb |
| Descriptor | Protein O-GlcNAcase, (5R,6R,7R,8S)-8-(ACETYLAMINO)-6,7-DIHYDROXY-5-(HYDROXYMETHYL)-N-PHENYL-1,5,6,7,8,8A-HEXAHYDROIMIDAZO[1,2-A]PYRIDINE-2-CARBOXAMIDE (2 entities in total) |
| Functional Keywords | human glacoside hydrolase, glcnac, hydrolase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Isoform 3: Nucleus . Isoform 1: Cytoplasm : O60502 |
| Total number of polymer chains | 2 |
| Total formula weight | 206764.56 |
| Authors | Roth, C.,Chan, S.,Offen, W.A.,Hemsworth, G.R.,Willems, L.I.,King, D.,Varghese, V.,Britton, R.,Vocadlo, D.J.,Davies, G.J. (deposition date: 2016-10-28, release date: 2017-03-29, Last modification date: 2024-11-20) |
| Primary citation | Roth, C.,Chan, S.,Offen, W.A.,Hemsworth, G.R.,Willems, L.I.,King, D.T.,Varghese, V.,Britton, R.,Vocadlo, D.J.,Davies, G.J. Structural and functional insight into human O-GlcNAcase. Nat. Chem. Biol., 13:610-612, 2017 Cited by PubMed Abstract: O-GlcNAc hydrolase (OGA) removes O-linked N-acetylglucosamine (O-GlcNAc) from a myriad of nucleocytoplasmic proteins. Through co-expression and assembly of OGA fragments, we determined the three-dimensional structure of human OGA, revealing an unusual helix-exchanged dimer that lays a structural foundation for an improved understanding of substrate recognition and regulation of OGA. Structures of OGA in complex with a series of inhibitors define a precise blueprint for the design of inhibitors that have clinical value. PubMed: 28346405DOI: 10.1038/nchembio.2358 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
Download full validation report
