Research workbench
Solution NMR structure of the filamin-migfilin complex
Analyse Solution NMR structure of the filamin-migfilin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K9U
- Type
- protein
- Length
- 143 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gamma filamin; Filamin-binding lim protein 1
- UniProt
- Q59H94, Q8WUP2
- Pockets
- 2 · best druggability 0.74
Structure
solution nmr · 2 distinct chains · 0% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gamma filamin | protein | 119 | 0% helix, 40% strand | Q59H94 |
| B | Filamin-binding lim protein 1 | protein | 24 | 0% helix, 33% strand | Q8WUP2 |
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 | 79 | 0.74 | 0.96 | 21 | empty |
| 2 | 131 | 0.50 | 0.79 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 618 Ų buried · 18 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 Q59H94
- Every structure of UniProt Q8WUP2
- Elsewhere: RCSB PDB 2K9U · PDBe 2K9U · UniProt Q59H94 · UniProt Q8WUP2
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