human POGLUT1 in complex with EGF(+) and UDP. Determined by X-ray diffraction at 1.43 Å resolution. Released 9 Aug 2017.
Explore 5L0T in 3D Show helices and sheets RCSB PDB PDBe
5L0T contains 30 α-helices and 27 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 |
|---|---|---|---|
| α-helix | 33-45 | 13 | |
| α-helix | 54-57 | 4 | |
| α-helix | 58-65 | 8 | |
| α-helix | 66-68 | 3 | |
| β-strand | 72 | 1 | 1 |
| α-helix | 74-82 | 9 | |
| β-strand | 87-92 | 6 | 2 |
| β-strand | 95-98 | 4 | 2 |
| α-helix | 105-118 | 14 | |
| α-helix | 119-121 | 3 | |
| α-helix | 122-123 | 2 | |
| β-strand | 125-129 | 5 | 2 |
| β-strand | 138 | 1 | 3 |
| β-strand | 148-149 | 2 | 2 |
| β-strand | 152 | 1 | 4 |
| β-strand | 156 | 1 | 3 |
| α-helix | 158 | 1 | |
| β-strand | 159-160 | 2 | 2 |
| α-helix | 164-166 | 3 | |
| α-helix | 184-197 | 14 | |
| α-helix | 200-202 | 3 | |
| β-strand | 204 | 1 | 5 |
| β-strand | 207-211 | 5 | 6 |
| α-helix | 216-218 | 3 | |
| α-helix | 219-227 | 9 | |
| β-strand | 232-236 | 5 | 6 |
| β-strand | 237 | 1 | 7 |
| α-helix | 238 | 1 | |
| α-helix | 245-248 | 4 | |
| α-helix | 252-253 | 2 | |
| β-strand | 254 | 1 | 7 |
| α-helix | 255-256 | 2 | |
| α-helix | 259-262 | 4 | |
| β-strand | 265 | 1 | 5 |
| β-strand | 267-270 | 4 | 6 |
| α-helix | 279-285 | 7 | |
| α-helix | 288 | 1 | |
| β-strand | 289-293 | 5 | 6 |
| β-strand | 298 | 1 | 4 |
| α-helix | 302-304 | 3 | |
| β-strand | 307 | 1 | 8 |
| β-strand | 311 | 1 | 8 |
| β-strand | 312-314 | 3 | 6 |
| α-helix | 321-330 | 10 | |
| α-helix | 332-349 | 18 | |
| α-helix | 352-367 | 16 | |
| β-strand | 370 | 1 | 1 |
| α-helix | 376-377 | 2 | |
| α-helix | 380 | 1 | |
| β-strand | 381-383 | 3 | 2 |
| α-helix | 384 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-7 | 4 | |
| β-strand | 15-18 | 4 | 9 |
| β-strand | 23-26 | 4 | 9 |
| α-helix | 27-28 | 2 | |
| β-strand | 31-32 | 2 | 10 |
| β-strand | 38-39 | 2 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein O-glucosyltransferase 1 | A | protein | 357 | Homo sapiens | Q8NBL1 (AlphaFold model) |
| EGF(+) | B | protein | 42 | synthetic construct |
>5L0T_1 Protein O-glucosyltransferase 1 (chains A) GSKWKVFIDQINRSLENYEPCSSQNCSCYHGVIEEDLTPFRGGISRKMMAEVVRRKLGTH YQITKNRLYRENDCMFPSRCSGVEHFILEVIGRLPDMEMVINVRDYPQVPKWMEPAIPVF SFSKTSEYHDIMYPAWTFWEGGPAVWPIYPTGLGRWDLFREDLVRSAAQWPWKKKNSTAY FRGSRTSPERDPLILLSRKNPKLVDAEYTKNQAWKSMKDTLGKPAAKDVHLVDHCKYKYL FNFRGVAASFRFKHLFLCGSLVFHVGDEWLEFFYPQLKPWVHYIPVKTDLSNVQELLQFV KANDDVAQEIAERGSQFIRNHLQMDDITCYWENLLSEYSKFLSYNVTRRKGYDQIIP
>5L0T_2 EGF(+) (chains B) GSDIDECASNPCQNGGTCVNTVGSYTCLCPPGFTGPNCEDDI
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 3 |
| UDP | Uridine-5'-diphosphate | C9 H14 N2 O12 P2 | 1 |
| CA | Calcium ion | Ca | 3 |
Water and common crystallization additives (CL, GOL) are not listed.
Structural basis of Notch O-glucosylation and O-xylosylation by mammalian protein-O-glucosyltransferase 1 (POGLUT1). Li, Z., Fischer, M., Satkunarajah, M. et al. Nat Commun (2017) 8:185-185. DOI 10.1038/s41467-017-00255-7 · PubMed
Other PDB entries of the same protein (UniProt Q8NBL1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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