Research workbench
Cardiac muscle myosin motor domain in the pre-powerstroke state
Analyse Cardiac muscle myosin motor domain in the pre-powerstroke state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N6A
- Type
- protein
- Length
- 710 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin-7
- UniProt
- Q9BE39
- Ligands
- ADP, MG, PO4
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin-7 | protein | 710 | 36% helix, 14% strand | Q9BE39 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 802 | 0.73 | 0.78 | 69 | empty |
| 2 | 380 | 0.70 | 0.83 | 51 | ADP, PO4, MG |
| 3 | 562 | 0.65 | 0.76 | 49 | empty |
| 4 | 234 | 0.59 | 0.79 | 28 | empty |
| 5 | 61 | 0.37 | 0.79 | 19 | empty |
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 Q9BE39
- Elsewhere: RCSB PDB 5N6A · PDBe 5N6A · UniProt Q9BE39
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