Research workbench
Structure of the actin-binding domain of human filamin a mutant E254K
Analyse Structure of the actin-binding domain of human filamin a mutant E254K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HOC
- Type
- protein
- Length
- 432 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Filamin-a
- UniProt
- P21333
- Ligands
- PO4
- Pockets
- 2 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Filamin-a | protein | 215 | 60% helix, 0% strand | P21333 |
| B | Filamin-a | protein | 217 | 58% helix, 0% strand | P21333 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 862 | 0.76 | 0.80 | 80 | empty |
| 2 | 66 | 0.32 | 0.76 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 626 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 3HOC · PDBe 3HOC · UniProt P21333
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