Research workbench
Structure of the actin-tropomyosin-myosin complex (rigor atm 3)
Analyse Structure of the actin-tropomyosin-myosin complex (rigor atm 3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A7F
- Type
- protein
- Length
- 4,214 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha skeletal muscle; Tropomyosin 1 alpha; Myosin ie heavy chain
- EC
- 3.6.4.1
- UniProt
- P68135, P58772, Q03479
- Ligands
- ADP, CA
- Pockets
- 20 · best druggability 0.92
Structure
electron microscopy · 3 distinct chains · 44% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E, F, I | Actin, alpha skeletal muscle | protein | 375 | 34% helix, 12% strand | P68135 |
| B, H | Tropomyosin 1 alpha | protein | 136 | 99% helix, 0% strand | P58772 |
| C, G, J | Myosin ie heavy chain (EC 3.6.4.1) | protein | 689 | 38% helix, 9% strand | Q03479 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, D, E, F, I
- CA · Calcium ion · metal · 5 copies · chains A, D, E, F, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1040 | 0.92 | 0.94 | 151 | empty |
| 2 | 1166 | 0.90 | 0.91 | 144 | empty |
| 3 | 811 | 0.89 | 0.92 | 109 | empty |
| 4 | 961 | 0.87 | 0.88 | 157 | empty |
| 5 | 662 | 0.87 | 0.91 | 91 | ADP, CA |
Interfaces
23 interfaces between chains.
- B–H · 3426 Ų buried · 11 hydrogen bonds · protein-protein
- G–I · 1576 Ų buried · 6 hydrogen bonds · protein-protein
- D–J · 1565 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 1560 Ų buried · 8 hydrogen bonds · protein-protein
- A–I · 1023 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (methylation).
Compared structures
- 4A7F · Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3) · the same entry in another collection · chain J against J, TM-score 1.00
- P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain E against A, TM-score 0.91
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
- Every structure of UniProt P58772
- Every structure of UniProt Q03479
- Elsewhere: RCSB PDB 4A7F · PDBe 4A7F · UniProt P68135 · UniProt P58772 · UniProt Q03479
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