Research workbench
Myosin VI (md) pre-powerstroke state, P21 crystal form
Analyse Myosin VI (md) pre-powerstroke state, P21 crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E7Z
- Type
- protein
- Length
- 1,504 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin-VI
- UniProt
- F1RQI7
- Ligands
- ADP, MG, VO4
- Pockets
- 15 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin-VI | protein | 759 | 48% helix, 16% strand | F1RQI7 |
| B | Myosin-VI | protein | 745 | 46% helix, 15% 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
- GOL · Glycerol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 922 | 0.79 | 0.81 | 94 | empty |
| 2 | 764 | 0.75 | 0.80 | 82 | empty |
| 3 | 473 | 0.74 | 0.83 | 54 | ADP, VO4, MG, GOL |
| 4 | 475 | 0.73 | 0.83 | 56 | ADP, VO4, MG |
| 5 | 149 | 0.69 | 0.89 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 420 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4E7Z · Myosin VI (MD) pre-powerstroke state, P21 crystal form · 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 4E7Z · PDBe 4E7Z · UniProt F1RQI7
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