5M7S

Structure of human O-GlcNAc hydrolase with bound transition state analog ThiametG

Summary for 5M7S

• Entry DOI: 10.2210/pdb5m7s/pdb
• Descriptor: Protein O-GlcNAcase, (3AR,5R,6S,7R,7AR)-2-(ETHYLAMINO)-5-(HYDROXYMETHYL)-5,6,7,7A-TETRAHYDRO-3AH-PYRANO[3,2-D][1,3]THIAZOLE-6,7-DIOL (3 entities in total)
• Functional Keywords: hoga o-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: 206538.41

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: 2024-11-06)

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

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: 28346405
DOI: 10.1038/nchembio.2358

Experimental method

X-RAY DIFFRACTION (2.4 Å)