Human OGT in complex with UDP and fused substrate peptide (HCF1). Determined by X-ray diffraction at 1.9 Å resolution. Released 12 Jul 2017.
Explore 5LWV in 3D Show helices and sheets RCSB PDB PDBe
5LWV contains 44 α-helices and 22 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 |
|---|---|---|---|
| α-helix | 299-302 | 4 | |
| α-helix | 307-310 | 4 | |
| α-helix | 315-329 | 15 | |
| α-helix | 333-346 | 14 | |
| α-helix | 351-363 | 13 | |
| α-helix | 367-380 | 14 | |
| α-helix | 385-397 | 13 | |
| α-helix | 401-414 | 14 | |
| α-helix | 419-432 | 14 | |
| α-helix | 435-448 | 14 | |
| α-helix | 453-465 | 13 | |
| α-helix | 472-488 | 17 | |
| α-helix | 497-500 | 4 | |
| α-helix | 507-526 | 20 | |
| α-helix | 530-536 | 7 | |
| α-helix | 540-542 | 3 | |
| β-strand | 546-552 | 7 | 1 |
| α-helix | 559-564 | 6 | |
| α-helix | 567-570 | 4 | |
| β-strand | 576-582 | 7 | 1 |
| α-helix | 590-598 | 9 | |
| β-strand | 601-604 | 4 | 1 |
| α-helix | 605-607 | 3 | |
| α-helix | 611-620 | 10 | |
| β-strand | 625-628 | 4 | 1 |
| α-helix | 639-642 | 4 | |
| β-strand | 648-651 | 4 | 1 |
| β-strand | 666-669 | 4 | 1 |
| α-helix | 676-681 | 6 | |
| β-strand | 685-688 | 4 | 1 |
| α-helix | 698-701 | 4 | |
| α-helix | 703-705 | 3 | |
| β-strand | 709-711 | 3 | 2 |
| β-strand | 724-727 | 4 | 2 |
| α-helix | 731-736 | 6 | |
| β-strand | 742-743 | 2 | 2 |
| β-strand | 765-767 | 3 | 2 |
| α-helix | 771-781 | 11 | |
| β-strand | 786-789 | 4 | 2 |
| β-strand | 792-796 | 5 | 2 |
| α-helix | 800-803 | 4 | |
| α-helix | 805-808 | 4 | |
| β-strand | 817-821 | 5 | 2 |
| α-helix | 822-825 | 4 | |
| β-strand | 833-836 | 4 | 3 |
| α-helix | 840-842 | 3 | |
| α-helix | 845-857 | 13 | |
| β-strand | 862-867 | 6 | 3 |
| α-helix | 870-872 | 3 | |
| α-helix | 873-882 | 10 | |
| α-helix | 887-889 | 3 | |
| β-strand | 890-894 | 5 | 3 |
| α-helix | 898-904 | 7 | |
| α-helix | 905-907 | 3 | |
| β-strand | 910-912 | 3 | 3 |
| α-helix | 921-928 | 8 | |
| β-strand | 933-934 | 2 | 3 |
| β-strand | 935 | 1 | 4 |
| α-helix | 941-943 | 3 | |
| α-helix | 945-953 | 9 | |
| α-helix | 956-958 | 3 | |
| β-strand | 959 | 1 | 4 |
| α-helix | 963-975 | 13 | |
| α-helix | 977-993 | 17 | |
| α-helix | 999-1018 | 20 | |
| β-strand | 1026 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Host cell factor 1,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit | A | protein | 749 | Homo sapiens | O15294 (AlphaFold model), P51610 (AlphaFold model) |
>5LWV_1 Host cell factor 1,UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (chains A) HHHHHHPPCETHETGTTNTATTATGGGTHADSLNNLANIKREQGNIEEAVRLYRKALEVF PEFAAAHSNLASVLQQQGKLQEALMHYKEAIRISPTFADAYSNMGNTLKEMQDVQGALQC YTRAIQINPAFADAHSNLASIHKDSGNIPEAIASYRTALKLKPDFPDAYCNLAHCLQIVC DWTDYDERMKKLVSIVADQLEKNRLPSVHPHHSMLYPLSHGFRKAIAERHGNLCLDKINV LHKPPYEHPKDLKLSDGRLRVGYVSSDFGNHPTSHLMQSIPGMHNPDKFEVFCYALSPDD GTNFRVKVMAEANHFIDLSQIPCNGKAADRIHQDGIHILVNMNGYTKGARNELFALRPAP IQAMWLGYPGTSGALFMDYIITDQETSPAEVAEQYSEKLAYMPHTFFIGDHANMFPHLKK KAVIDFKSNGHIYDNRIVLNGIDLKAFLDSLPDVKIVKMKCPDGGDNADSSNTALNMPVI PMNTIAEAVIEMINRGQIQITINGFSISNGLATTQINNKAATGEEVPRTIIVTTRSQYGL PEDAIVYCNFNQLYKIDPSTLQMWANILKRVPNSVLWLLRFPAVGEPNIQQYAQNMGLPQ NRIIFSPVAPKEEHVRRGQLADVCLDTPLCNGHTTGMDVLWAGTPMVTMPGETLASRVAA SQLTCLGCLELIAKNRQEYEDIAVKLGTDLEYLKKVRGKVWKQRISSPLFNTKQYTMELE RLYLQMWEHYAAGNKPDHMIKPVEVTESA
Water and common crystallization additives (GOL) are not listed.
Recognition of a glycosylation substrate by the O-GlcNAc transferase TPR repeats. Rafie, K., Raimi, O., Ferenbach, A.T. et al. Open Biol (2017) 7. DOI 10.1098/rsob.170078 · PubMed
Other PDB entries of the same protein (UniProt O15294 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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