Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GalNac-beta1,3-GlcNAc-beta-pNP. Determined by X-ray diffraction at 1.5 Å resolution. Released 10 Aug 2016.
Explore 5GGO in 3D Show helices and sheets RCSB PDB PDBe
5GGO contains 12 α-helices and 20 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 98-105 | 8 | 1 |
| β-strand | 106 | 1 | 2 |
| β-strand | 110-114 | 5 | 1 |
| β-strand | 117-122 | 6 | 1 |
| β-strand | 130-136 | 7 | 2 |
| β-strand | 143-149 | 7 | 2 |
| α-helix | 156-166 | 11 | |
| α-helix | 168 | 1 | |
| β-strand | 172-178 | 7 | 2 |
| α-helix | 187-195 | 9 | |
| α-helix | 201-203 | 3 | |
| β-strand | 209-215 | 7 | 2 |
| β-strand | 220-226 | 7 | 2 |
| α-helix | 235-237 | 3 | |
| β-strand | 238-245 | 8 | 1 |
| α-helix | 246-247 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 99-105 | 7 | 3 |
| β-strand | 106 | 1 | 4 |
| β-strand | 110-114 | 5 | 3 |
| β-strand | 117-122 | 6 | 3 |
| β-strand | 130-136 | 7 | 4 |
| β-strand | 143-149 | 7 | 4 |
| α-helix | 156-166 | 11 | |
| α-helix | 168 | 1 | |
| α-helix | 171 | 1 | |
| β-strand | 172-178 | 7 | 4 |
| α-helix | 187-195 | 9 | |
| α-helix | 201-203 | 3 | |
| β-strand | 209-215 | 7 | 4 |
| β-strand | 220-226 | 7 | 4 |
| α-helix | 235-237 | 3 | |
| β-strand | 238-244 | 7 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 | A, B | protein | 164 | Homo sapiens | Q8WZA1 (AlphaFold model) |
>5GGO_1 Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (chains A, B) GPLGSGSGPRRVLDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAK RVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGW RDTWAFVGRKGGPVFGEKHSKSPALSSWGDPVLLKTDVPLSSAE
Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of alpha-dystroglycan. Kuwabara, N., Manya, H., Yamada, T. et al. Proc Natl Acad Sci U S A (2016) 113:9280-9285. DOI 10.1073/pnas.1525545113 · PubMed
Other PDB entries of the same protein (UniProt Q8WZA1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 5GGO directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.