Research workbench
Cryo-EM structure of the ADP state actin filament
Analyse Cryo-EM structure of the ADP state actin filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7R8V
- Type
- protein
- Length
- 1,855 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle, intermediate form
- UniProt
- P68139
- Ligands
- ADP, MG
- Pockets
- 17 · best druggability 0.82
Structure
electron microscopy · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A, C, D, E | Actin, alpha skeletal muscle, intermediate form | protein | 371 | 43% helix, 20% strand | P68139 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains B, A, C, D, E
- MG · Magnesium ion · metal · 5 copies · chains B, A, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 973 | 0.82 | 0.83 | 89 | empty |
| 2 | 765 | 0.80 | 0.83 | 81 | empty |
| 3 | 278 | 0.78 | 0.90 | 54 | ADP, MG |
| 4 | 285 | 0.77 | 0.89 | 55 | ADP, MG |
| 5 | 364 | 0.76 | 0.87 | 59 | ADP, MG |
Interfaces
7 interfaces between chains.
- D–E · 1224 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 1224 Ų buried · 13 hydrogen bonds · protein-protein
- B–A · 1217 Ų buried · 13 hydrogen bonds · protein-protein
- A–D · 446 Ų buried · 4 hydrogen bonds · protein-protein
- B–E · 445 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 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
- Elsewhere: RCSB PDB 7R8V · PDBe 7R8V · UniProt P68139
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