O-GlcNAc transferase

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Template:STRUCTURE 1nlm


O-GlcNac transferase (OGT) catalyzes the addition of N-acetylglucosamine (GlcNAc) to serine or threonine residues by O-glycosylation. For details see Human O-GlcNac transferase.

Contents

3D structures of O-GlcNAc transferase

1fo8, 1fo9, 1foa - rOGT catalytic domain – rabbit

1w3b – hOGT TPR domain – human

2gak – mOGT – mouse

2j0a, 3otk – mOGT catalytic domain (mutant)

OGT binary complexes

2am3, 2am4 - rOGT catalytic domain + UDP-glucose derivative

2am5 - rOGT catalytic domain + UDP

2j0b - mOGT catalytic domain (mutant) + UDP

2apc - rOGT catalytic domain + UDP-GlcNAc phosphonate

2gam - mOGT + b-D-galactose + N-acetyl-galactosamine

3pe3, 3pe4 – hOGT residues 323-1041 + peptide substrate

2jlb – XcOGT + UDP-GlcNAc phosphonate analog – Xanthomonas campestris

2xgm – XcOGT + alloxan + mesoxalylurea

2xgc - XcOGT + UDP-GlcNAc

2xgs - XcOGT + UDP

1nlm – OGT + UDP-acetylglucosamine – Escherichia coli

3ee5 – hOGT + UDP + NAG + galactose + naphthalene derivative

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

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