Research workbench
T-plastin-F-actin complex
Analyse T-plastin-F-actin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R94
- Type
- protein
- Length
- 2,570 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Plastin-3
- UniProt
- P68139, P13797
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 2 distinct chains · 48% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, B, A, D, E | Actin, alpha skeletal muscle | protein | 370 | 44% helix, 20% strand | P68139 |
| F, G, H | Plastin-3 | protein | 240 | 53% helix, 0% strand | P13797 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains C, B, A, D, E
- MG · Magnesium ion · metal · 5 copies · chains C, B, A, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1133 | 0.80 | 0.81 | 85 | empty |
| 2 | 703 | 0.78 | 0.83 | 76 | empty |
| 3 | 304 | 0.77 | 0.88 | 52 | ADP, MG |
| 4 | 312 | 0.76 | 0.88 | 49 | ADP, MG |
| 5 | 292 | 0.76 | 0.88 | 52 | ADP, MG |
Interfaces
13 interfaces between chains.
- C–A · 1207 Ų buried · 10 hydrogen bonds · protein-protein
- C–E · 1198 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 1197 Ų buried · 10 hydrogen bonds · protein-protein
- B–H · 892 Ų buried · 9 hydrogen bonds · protein-protein
- C–G · 890 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified, 3 covalent (methylation, covalent ligand).
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 P68139
- Every structure of UniProt P13797
- Elsewhere: RCSB PDB 7R94 · PDBe 7R94 · UniProt P68139 · UniProt P13797
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