MolNFT v1 · #115391 · protein
Structure of ULK1 bound to a selective inhibitor
5CI7 · SERINE/THREONINE-protein kinase ULK1: “Structure of ULK1 bound to a selective inhibitor”. X-ray diffraction, 1 ligand (51W), 2 pockets (best druggability 0.65). MolNFT v1 #115391 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 5CI7
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SERINE/THREONINE-protein kinase ULK1
- EC
- 2.7.11.1
- UniProt
- O75385
- Ligands
- 51W
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SERINE/THREONINE-protein kinase ULK1 (EC 2.7.11.1) | protein | 277 | 36% helix, 21% strand | O75385 |
Ligands and binding sites
- 51W · N-[3-({4-[(3-aminopropyl)amino]-5-iodopyrimidin-2-yl}amino)phenyl]pyrrolidine-1-carboxamide · ligand · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 297 | 0.65 | 0.81 | 32 | 51W, GOL |
| 2 | 61 | 0.35 | 0.78 | 17 | empty |
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O75385
- Elsewhere: RCSB PDB 5CI7 · PDBe 5CI7 · UniProt O75385
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