Research workbench
Myosin VI D23R I24R R569E (md) pre-powerstroke state
Analyse Myosin VI D23R I24R R569E (md) 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
- 4E7S
- Type
- protein
- Length
- 1,514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin-VI
- UniProt
- F1RQI7
- Ligands
- ADP, MG, VO4, PO4
- Pockets
- 14 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin-VI | protein | 762 | 46% helix, 16% strand | F1RQI7 |
| B | Myosin-VI | protein | 752 | 48% helix, 16% strand | F1RQI7 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- VO4 · Vanadate ion · ion · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · chains B
- GOL · Glycerol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1097 | 0.82 | 0.83 | 89 | GOL |
| 2 | 739 | 0.75 | 0.80 | 84 | empty |
| 3 | 494 | 0.73 | 0.82 | 55 | ADP, VO4, MG |
| 4 | 441 | 0.73 | 0.83 | 51 | ADP, VO4, MG |
| 5 | 532 | 0.72 | 0.80 | 61 | empty |
Interfaces
1 interface between chains.
- A–B · 702 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4E7S · Myosin VI D23R I24R R569E (MD) pre-powerstroke state · the same entry in another collection · chain A against A, TM-score 1.00
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 F1RQI7
- Elsewhere: RCSB PDB 4E7S · PDBe 4E7S · UniProt F1RQI7
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