MolNFT v1 · #151887 · protein
Crystal structure of fascin in complex with compound 5
6I12: “Crystal structure of fascin in complex with compound 5”. X-ray diffraction, 1 ligand (H08), 3 pockets (best druggability 0.65). MolNFT v1 #151887 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6I12
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fascin
- UniProt
- Q16658
- Ligands
- H08
- Pockets
- 3 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fascin | protein | 484 | 6% helix, 46% strand | Q16658 |
Ligands and binding sites
- H08 · 2-[(4-chlorophenyl)methyl]-~{N}-(1-methylpyrazol-4-yl)-1-oxidanylidene-isoquinoline-4-carboxamide · ligand · 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 | 233 | 0.65 | 0.83 | 36 | ACT, H08 |
| 2 | 246 | 0.55 | 0.77 | 43 | empty |
| 3 | 86 | 0.34 | 0.74 | 25 | 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 6I12 · PDBe 6I12 · UniProt Q16658
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