Research workbench
Crystal structure of filamin-a immunoglobulin-like repeat 21 bound to an N-terminal peptide of cftr
Analyse Crystal structure of filamin-a immunoglobulin-like repeat 21 bound to an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ISW
- Type
- protein
- Length
- 205 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Filamin-a; Cystic fibrosis transmembrane conductance regulator
- UniProt
- P21333, P13569
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Filamin-a | protein | 93 | 6% helix, 56% strand | P21333 |
| B | Filamin-a | protein | 94 | 6% helix, 55% strand | P21333 |
| C | Cystic fibrosis transmembrane conductance regulator | protein | 18 | 0% helix, 50% strand | P13569 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 181 | 0.64 | 0.84 | 25 | empty |
Interfaces
3 interfaces between chains.
- A–C · 655 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 475 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 327 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 3ISW · Crystal structure of filamin-A immunoglobulin-like repeat 21 bound to an N-terminal… · the same entry in another collection · chain A against A, TM-score 1.00
- P21333 · AlphaFold monomer V2.0 prediction for filamin-a (P21333) · a predicted model of the same protein · chain B against A, TM-score 0.95
- P13569 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain C against A, TM-score 0.27
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
- Every structure of UniProt P13569
- Elsewhere: RCSB PDB 3ISW · PDBe 3ISW · UniProt P21333 · UniProt P13569
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