Kinase domain of mutant human ULK1 in complex with compound XMD-17-51. Determined by X-ray diffraction at 1.83 Å resolution. Released 5 Jun 2024.
Explore 8P5I in 3D Show helices and sheets RCSB PDB PDBe
8P5I contains 51 α-helices and 56 β-strands across 4 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 | 9-11 | 3 | 1 |
| β-strand | 14-25 | 12 | 1 |
| β-strand | 28-35 | 8 | 1 |
| β-strand | 42-47 | 6 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 53-67 | 15 | |
| β-strand | 75 | 1 | 2 |
| β-strand | 78-83 | 6 | 1 |
| β-strand | 88-92 | 5 | 1 |
| β-strand | 99 | 1 | 2 |
| α-helix | 100-107 | 8 | |
| α-helix | 112-132 | 21 | |
| β-strand | 134-135 | 2 | 3 |
| α-helix | 141-143 | 3 | |
| β-strand | 144-147 | 4 | 2 |
| β-strand | 160-163 | 4 | 2 |
| β-strand | 170-171 | 2 | 3 |
| β-strand | 178 | 1 | 4 |
| α-helix | 185-187 | 3 | |
| α-helix | 190-193 | 4 | |
| β-strand | 198 | 1 | 4 |
| α-helix | 201-216 | 16 | |
| α-helix | 226-235 | 10 | |
| α-helix | 249-258 | 10 | |
| α-helix | 269-273 | 5 | |
| α-helix | 276-278 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-11 | 3 | 5 |
| β-strand | 14-25 | 12 | 5 |
| β-strand | 28-35 | 8 | 5 |
| β-strand | 42-47 | 6 | 5 |
| α-helix | 50-52 | 3 | |
| α-helix | 53-67 | 15 | |
| β-strand | 75 | 1 | 6 |
| β-strand | 78-84 | 7 | 5 |
| β-strand | 88-93 | 6 | 5 |
| β-strand | 99 | 1 | 6 |
| α-helix | 100-107 | 8 | |
| α-helix | 112-132 | 21 | |
| β-strand | 134-135 | 2 | 7 |
| α-helix | 141-143 | 3 | |
| β-strand | 144-147 | 4 | 6 |
| β-strand | 160-163 | 4 | 6 |
| β-strand | 170-171 | 2 | 7 |
| β-strand | 178 | 1 | 8 |
| α-helix | 185-187 | 3 | |
| α-helix | 190-193 | 4 | |
| β-strand | 198 | 1 | 8 |
| α-helix | 201-216 | 16 | |
| α-helix | 226-235 | 10 | |
| α-helix | 249-258 | 10 | |
| α-helix | 263-265 | 3 | |
| α-helix | 269-273 | 5 | |
| α-helix | 276-278 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-11 | 3 | 1 |
| β-strand | 14-25 | 12 | 1 |
| β-strand | 28-35 | 8 | 1 |
| β-strand | 42-47 | 6 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 53-67 | 15 | |
| β-strand | 75 | 1 | 12 |
| β-strand | 78-83 | 6 | 1 |
| β-strand | 88-93 | 6 | 1 |
| β-strand | 99 | 1 | 12 |
| α-helix | 100-107 | 8 | |
| α-helix | 112-132 | 21 | |
| β-strand | 134-135 | 2 | 13 |
| α-helix | 141-143 | 3 | |
| β-strand | 144-147 | 4 | 12 |
| α-helix | 156-158 | 3 | |
| β-strand | 160-163 | 4 | 12 |
| β-strand | 170-171 | 2 | 13 |
| β-strand | 178 | 1 | 14 |
| α-helix | 185-187 | 3 | |
| α-helix | 190-193 | 4 | |
| β-strand | 198 | 1 | 14 |
| α-helix | 201-216 | 16 | |
| α-helix | 226-235 | 10 | |
| α-helix | 249-258 | 10 | |
| α-helix | 269-273 | 5 | |
| α-helix | 276-278 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Serine/threonine-protein kinase ULK1 | A, B, C, D | protein | 284 | Homo sapiens | O75385 (AlphaFold model) |
>8P5I_1 Serine/threonine-protein kinase ULK1 (chains A, B, C, D) SMEPGRGGTETVGKFEFSRKDLIGHGAFAVVFKGRHREKHDLEVAVKCINKKNLAKSQTL LGKEIKILKELKHENIVALYDFQEMANSVYLVMEYCNGGDLADYLHAMRTLSEDTIRLFL QQIAGAMRLLHSKGIIHRDLKPQNILLSNPAGRRANPNSIRVKIADFGFARYLQSNMMAA TLCGSPMYMAPEVIMSQHYDGKADLWSIGTIVYQCLTGKAPFQASSPQDLRLFYEKNKTL VPTIPAATSAPLRQLLLALLQRNHKDRMDFDEFFHHPFLDASPS
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 8 |
| WYX | 5,11-dimethyl-2-[(1-piperidin-4-ylpyrazol-4-yl)amino]pyrimido[4,5-b][1,4]benzod… | C21 H24 N8 O | 4 |
Water and common crystallization additives (GOL, NA) are not listed.
Crystal structures of ULK1 in complex with KCGS compounds. Battista, T., Semrau, M.S., Lolli, G. et al. To be published.
Other PDB entries of the same protein (UniProt O75385 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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