Crystal structure of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase form I. Determined by X-ray diffraction at 3.0 Å resolution. Released 10 Aug 2016.
Explore 5GGG in 3D Show helices and sheets RCSB PDB PDBe
5GGG contains 29 α-helices and 30 β-strands across 1 chain. 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 | 117-120 | 4 | 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 | 186-195 | 10 | |
| 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 | 246-248 | 3 | |
| α-helix | 260-269 | 10 | |
| α-helix | 276-279 | 4 | |
| α-helix | 284-286 | 3 | |
| α-helix | 291-293 | 3 | |
| β-strand | 304-308 | 5 | 3 |
| α-helix | 312-323 | 12 | |
| α-helix | 330-332 | 3 | |
| β-strand | 333-338 | 6 | 3 |
| α-helix | 342-350 | 9 | |
| β-strand | 354-358 | 5 | 3 |
| α-helix | 364-382 | 19 | |
| β-strand | 388-393 | 6 | 3 |
| β-strand | 396-398 | 3 | 4 |
| α-helix | 399 | 1 | |
| α-helix | 402-409 | 8 | |
| α-helix | 411-415 | 5 | |
| β-strand | 419-423 | 5 | 3 |
| β-strand | 430 | 1 | 5 |
| β-strand | 440-443 | 4 | 3 |
| β-strand | 451-454 | 4 | 3 |
| α-helix | 455-457 | 3 | |
| α-helix | 458-462 | 5 | |
| α-helix | 463-465 | 3 | |
| α-helix | 466-468 | 3 | |
| α-helix | 475-479 | 5 | |
| α-helix | 482-485 | 4 | |
| β-strand | 489-493 | 5 | 3 |
| β-strand | 496 | 1 | 6 |
| β-strand | 498-500 | 3 | 4 |
| β-strand | 520 | 1 | 5 |
| β-strand | 522 | 1 | 6 |
| α-helix | 533-536 | 4 | |
| α-helix | 538-551 | 14 | |
| β-strand | 553-554 | 2 | 7 |
| α-helix | 555 | 1 | |
| α-helix | 564-566 | 3 | |
| β-strand | 574-581 | 8 | 7 |
| α-helix | 588-596 | 9 | |
| β-strand | 607-608 | 2 | 7 |
| β-strand | 611-616 | 6 | 7 |
| β-strand | 619-627 | 9 | 7 |
| α-helix | 632-634 | 3 | |
| α-helix | 639-641 | 3 | |
| β-strand | 642 | 1 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 | A | protein | 578 | Homo sapiens | Q8WZA1 (AlphaFold model) |
>5GGG_1 Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (chains A) GSGPRRVLDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDT YSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWA FVGRKGGPVFGEKHSKSPALSSWGDPVLLKTDVPLSSAEEAECHWADTELNRRRRRFCSK VEGYGSVCSCKDPTPIEFSPDPLPDNKVLNVPVAVIAGNRPNYLYRMLRSLLSAQGVSPQ MITVFIDGYYEEPMDVVALFGLRGIQHTPISIKNARVSQHYKASLTATFNLFPEAKFAVV LEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAEDPALLYRVETMPGLGW VLRRSLYKEELEPKWPTPEKLWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMNGY FHEAYFKKHKFNTVPGVQLRNVDSLKKEAYEVEVHRLLSEAEVLDHSKNPCEDSFLPDTE GHTYVAFIRMEKDDDFTTWTQLAKCLHIWDLDVRGNHRGLWRLFRKKNHFLVVGVPASPY SVKKPPSVTPIFLEPPPKEEGAPGAPEQTLELEVLFQG
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:
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