Research workbench
Filamin a actin binding domain
Analyse Filamin a actin binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WFN
- Type
- protein
- Length
- 455 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Filamin-a
- UniProt
- P21333
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Filamin-a | protein | 227 | 54% helix, 0% strand | P21333 |
| B | Filamin-a | protein | 228 | 54% helix, 0% strand | P21333 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.68 | 0.84 | 36 | SO4 |
| 2 | 484 | 0.62 | 0.76 | 63 | empty |
| 3 | 292 | 0.55 | 0.76 | 34 | empty |
| 4 | 203 | 0.51 | 0.77 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1392 Ų buried · 12 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 P21333
- Elsewhere: RCSB PDB 2WFN · PDBe 2WFN · UniProt P21333
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