Research workbench
Cryo-EM structure of F-actin in the MG2+-ADP nucleotide state.
Analyse Cryo-EM structure of F-actin in the MG2+-ADP nucleotide state. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 8A2T
- Type
- protein
- Length
- 1,830 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle
- UniProt
- P68135
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 1 distinct chain · 44% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, A, B, D, E | Actin, alpha skeletal muscle | protein | 366 | 44% helix, 21% strand | P68135 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains C, A, B, D, E
- MG · Magnesium ion · metal · 5 copies · chains C, A, B, 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 | 527 | 0.79 | 0.86 | 72 | empty |
| 2 | 277 | 0.77 | 0.90 | 48 | ADP, MG |
| 3 | 279 | 0.77 | 0.89 | 48 | ADP, MG |
| 4 | 266 | 0.77 | 0.90 | 49 | ADP, MG |
| 5 | 269 | 0.76 | 0.89 | 47 | ADP, MG |
Interfaces
7 interfaces between chains.
- C–E · 1116 Ų buried · 13 hydrogen bonds · protein-protein
- C–A · 1108 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 1107 Ų buried · 12 hydrogen bonds · protein-protein
- C–B · 450 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 448 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (methylation).
Compared structures
- 8A2T · Cryo-EM structure of F-actin in the Mg2+-ADP nucleotide state. · 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 0.96
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 8A2T · PDBe 8A2T · UniProt P68135
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