Research workbench
Structure of fascin
Analyse Structure of fascin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P53
- Type
- protein
- Length
- 970 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fascin
- UniProt
- Q16658
- Pockets
- 11 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fascin | protein | 486 | 7% helix, 48% strand | Q16658 |
| B | Fascin | protein | 484 | 7% helix, 48% strand | Q16658 |
Ligands and binding sites
- GOL · Glycerol · additive · 8 copies · chains A, B
- 1PE · Pentaethylene glycol · additive · 5 copies · chains A, B
- 12P · Dodecaethylene glycol · additive · chains A
- PG0 · 2-(2-methoxyethoxy)ethanol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 619 | 0.73 | 0.80 | 44 | GOL |
| 2 | 386 | 0.66 | 0.80 | 61 | 1PE, PG0 |
| 3 | 512 | 0.66 | 0.78 | 67 | 1PE |
| 4 | 164 | 0.49 | 0.77 | 27 | empty |
| 5 | 94 | 0.45 | 0.80 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 592 Ų buried · 4 hydrogen bonds · protein-protein
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 3P53 · PDBe 3P53 · UniProt Q16658
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