Research workbench
T-plastin-F-actin complex, parallel bundled state
Analyse T-plastin-F-actin complex, parallel bundled state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SX8
- Type
- protein
- Length
- 2,668 residues
- Chains
- 7
- 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 0.83
Structure
electron microscopy · 2 distinct chains · 48% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, B, A, H, G, E | Actin, alpha skeletal muscle | protein | 370 | 39% helix, 16% strand | P68139 |
| D | Plastin-3 | protein | 448 | 55% helix, 0% strand | P13797 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains C, B, A, H, G, E
- MG · Magnesium ion · metal · 6 copies · chains C, B, A, H, G, 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, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 395 | 0.83 | 0.91 | 60 | ADP, MG |
| 2 | 1093 | 0.80 | 0.81 | 91 | empty |
| 3 | 312 | 0.79 | 0.90 | 56 | ADP, MG |
| 4 | 356 | 0.79 | 0.89 | 59 | ADP, MG |
| 5 | 231 | 0.79 | 0.92 | 47 | ADP, MG |
Interfaces
10 interfaces between chains.
- H–E · 1121 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 1109 Ų buried · 17 hydrogen bonds · protein-protein
- C–A · 1086 Ų buried · 7 hydrogen bonds · protein-protein
- D–E · 821 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 598 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (methylation).
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 7SX8 · PDBe 7SX8 · UniProt P68139 · UniProt P13797
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