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Crystal structure of fascin in complex with bdp-13176
Analyse Crystal structure of fascin in complex with bdp-13176 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6I18
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fascin
- UniProt
- Q16658
- Ligands
- H0N
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fascin | protein | 484 | 6% helix, 47% strand | Q16658 |
Ligands and binding sites
- H0N · 5-[(3,4-dichlorophenyl)methyl]-4-oxidanylidene-1-piperidin-4-yl-~{N}-pyridin-4-yl-pyrazolo[4,3-c]pyridine-7-carboxamide · ligand · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 275 | 0.65 | 0.81 | 38 | ACT, H0N |
| 2 | 270 | 0.54 | 0.76 | 44 | empty |
| 3 | 99 | 0.37 | 0.75 | 23 | empty |
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 Q16658
- Elsewhere: RCSB PDB 6I18 · PDBe 6I18 · UniProt Q16658
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