Research workbench
Cardiac actomyosin complex
Analyse Cardiac actomyosin complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7JH7
- Type
- protein
- Length
- 4,351 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Actin, alpha cardiac muscle 1; Myosin-7; Tropomyosin
- UniProt
- B6VNT8, P79293
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 3 distinct chains · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, E, D | Actin, alpha cardiac muscle 1 | protein | 371 | 38% helix, 16% strand | B6VNT8 |
| F, G, H | Myosin-7 | protein | 742 | 41% helix, 14% strand | P79293 |
| I, J | Tropomyosin | protein | 135 | 99% helix, 0% strand | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C, E, D
- MG · Magnesium ion · metal · 5 copies · chains A, B, C, E, D
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 | 1020 | 0.83 | 0.84 | 105 | empty |
| 2 | 845 | 0.82 | 0.84 | 87 | empty |
| 3 | 485 | 0.81 | 0.88 | 53 | empty |
| 4 | 501 | 0.80 | 0.87 | 55 | empty |
| 5 | 482 | 0.80 | 0.88 | 55 | empty |
Interfaces
22 interfaces between chains.
- I–J · 1485 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 1246 Ų buried · 12 hydrogen bonds · protein-protein
- B–G · 1242 Ų buried · 5 hydrogen bonds · protein-protein
- A–F · 1241 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 1233 Ų buried · 10 hydrogen bonds · protein-protein
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 B6VNT8
- Every structure of UniProt P79293
- Elsewhere: RCSB PDB 7JH7 · PDBe 7JH7 · UniProt B6VNT8 · UniProt P79293
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