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The crystal structure of human fascin 1 K358A mutant
Analyse The crystal structure of human fascin 1 K358A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GP3
- Type
- protein
- Length
- 961 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fascin
- UniProt
- Q16658
- Ligands
- CL, BR
- Pockets
- 11 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fascin | protein | 480 | 6% helix, 49% strand | Q16658 |
| B | Fascin | protein | 481 | 6% helix, 47% strand | Q16658 |
Ligands and binding sites
- CL · Chloride ion · ion · 18 copies · chains A, B
- BR · Bromide ion · ion · 7 copies · chains A, B
- GOL · Glycerol · additive · 7 copies · chains A, 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 592 | 0.71 | 0.79 | 44 | CL |
| 2 | 461 | 0.65 | 0.78 | 66 | empty |
| 3 | 226 | 0.50 | 0.75 | 30 | GOL |
| 4 | 139 | 0.49 | 0.79 | 36 | empty |
| 5 | 90 | 0.47 | 0.81 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 702 Ų buried · 2 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 4GP3 · PDBe 4GP3 · UniProt Q16658
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