MolNFT v1 · #148808 · protein
Cryo-EM structure of F-actin in complex with ADP-pi
6FHL · Actin, alpha skeletal muscle: “Cryo-EM structure of F-actin in complex with ADP-pi”. Electron microscopy, 3 ligands (ADP, MG, PO4), 17 pockets (best druggability 0.83). MolNFT v1 #148808 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6FHL
- Type
- protein
- Length
- 1,855 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle
- UniProt
- P68135
- Ligands
- ADP, MG, PO4
- Pockets
- 17 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E | Actin, alpha skeletal muscle | protein | 371 | 44% helix, 19% strand | P68135 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C, D, E
- MG · Magnesium ion · metal · 5 copies · chains A, B, C, D, E
- PO4 · Phosphate ion · ion · 5 copies · chains A, B, 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, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 776 | 0.83 | 0.86 | 110 | empty |
| 2 | 271 | 0.79 | 0.91 | 49 | ADP, MG, PO4 |
| 3 | 253 | 0.77 | 0.90 | 45 | ADP, MG, PO4 |
| 4 | 253 | 0.77 | 0.90 | 47 | ADP, MG, PO4 |
| 5 | 253 | 0.77 | 0.90 | 49 | ADP, MG, PO4 |
Interfaces
7 interfaces between chains.
- C–E · 1293 Ų buried · 17 hydrogen bonds · protein-protein
- A–C · 1288 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 1285 Ų buried · 16 hydrogen bonds · protein-protein
- D–E · 481 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 481 Ų buried · 2 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 P68135
- Elsewhere: RCSB PDB 6FHL · PDBe 6FHL · UniProt P68135
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