Research workbench
The structure of the actin filament uncapping complex mediated by twinfilin
Analyse The structure of the actin filament uncapping complex mediated by twinfilin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7CCC
- Type
- protein
- Length
- 1,574 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Twinfilin-1; F-actin-capping protein subunit alpha…
- UniProt
- P68135, Q12792, Q5RKN9, Q923G3
- Ligands
- ADP, CA
- Pockets
- 18 · best druggability 0.86
Structure
x-ray diffraction · 5 distinct chains · 41% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Actin, alpha skeletal muscle | protein | 357 | 45% helix, 20% strand | P68135 |
| B | Twinfilin-1 | protein | 342 | 37% helix, 25% strand | Q12792 |
| C | F-actin-capping protein subunit alpha | protein | 269 | 38% helix, 32% strand | Q5RKN9 |
| D | F-actin-capping protein subunit beta | protein | 248 | 38% helix, 34% strand | Q923G3 |
| E | Actin, alpha skeletal muscle | protein | 358 | 44% helix, 19% strand | P68135 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, E
- CA · Calcium ion · metal · 2 copies · chains A, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1023 | 0.86 | 0.87 | 113 | empty |
| 2 | 802 | 0.85 | 0.87 | 84 | empty |
| 3 | 390 | 0.76 | 0.86 | 55 | CA, ADP |
| 4 | 295 | 0.73 | 0.86 | 47 | CA, ADP |
| 5 | 304 | 0.71 | 0.85 | 41 | empty |
Interfaces
10 interfaces between chains.
- C–D · 3906 Ų buried · 49 hydrogen bonds · protein-protein
- A–B · 2187 Ų buried · 28 hydrogen bonds · protein-protein
- B–D · 2035 Ų buried · 24 hydrogen bonds · protein-protein
- B–E · 1458 Ų buried · 18 hydrogen bonds · protein-protein
- C–E · 503 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (methylation).
Compared structures
- 7CCC · The structure of the actin filament uncapping complex mediated by twinfilin · the same entry in another collection · chain E against E, TM-score 1.00
- P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain A against A, TM-score 0.95
- Q12792 · AlphaFold monomer V2.0 prediction for twinfilin-1 (Q12792) · a predicted model of the same protein · chain B against A, TM-score 0.60
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 P68135
- Every structure of UniProt Q12792
- Every structure of UniProt Q5RKN9
- Every structure of UniProt Q923G3
- Elsewhere: RCSB PDB 7CCC · PDBe 7CCC · UniProt P68135 · UniProt Q12792 · UniProt Q5RKN9 · UniProt Q923G3
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