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O-GlcNAc transferase

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{{STRUCTURE_1nlm| PDB=1nlm | SIZE=400| SCENE= |right|CAPTION=E. coli O-GlcNAc transferase dimer complex with UDP-GlcNAc and glycerol, [[1nlm]] }}
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{{STRUCTURE_1nlm| PDB=1nlm | SIZE=350| SCENE= |right|CAPTION=E. coli O-GlcNAc transferase dimer complex with UDP-GlcNAc and glycerol, [[1nlm]] }}
'''O-GlcNac transferase''' (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation. OGT contains 2 subunits: a 110 kDa and a 78kDa. The 110 kDa subunit contains a superhelical domain with 13 tetratricopeptide (TPR) repeats. The TPR motif consists of 34 amino acids and mediates protein-protein interactions. For details see [[Human O-GlcNAc transferase]].
'''O-GlcNac transferase''' (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation. OGT contains 2 subunits: a 110 kDa and a 78kDa. The 110 kDa subunit contains a superhelical domain with 13 tetratricopeptide (TPR) repeats. The TPR motif consists of 34 amino acids and mediates protein-protein interactions. For details see [[Human O-GlcNAc transferase]].
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==3D structures of O-GlcNAc transferase==
==3D structures of O-GlcNAc transferase==

Revision as of 12:02, 8 February 2016

Template:STRUCTURE 1nlm


O-GlcNac transferase (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation. OGT contains 2 subunits: a 110 kDa and a 78kDa. The 110 kDa subunit contains a superhelical domain with 13 tetratricopeptide (TPR) repeats. The TPR motif consists of 34 amino acids and mediates protein-protein interactions. For details see Human O-GlcNAc transferase.

3D structures of O-GlcNAc transferase

Updated on 08-February-2016

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