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Cryoem structure of myosin VI-actin complex in the ADP state, backbone-averaged with side chains truncated to alanine
Analyse Cryoem structure of myosin VI-actin complex in the ADP state, backbone-averaged… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BNW
- Type
- protein
- Length
- 7,580 residues
- Chains
- 14
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Unconventional myosin-VI; Actin, alpha skeletal muscle
- UniProt
- F1RQI7, P68135
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 2 distinct chains · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| I, J, K, L, M, N | Unconventional myosin-VI | protein | 774 | 44% helix, 15% strand | F1RQI7 |
| A, B, C, D, E, F, G, H | Actin, alpha skeletal muscle | protein | 367 | 39% helix, 20% strand | P68135 |
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 | 846 | 0.81 | 0.84 | 123 | empty |
| 2 | 1041 | 0.81 | 0.82 | 131 | empty |
| 3 | 1038 | 0.81 | 0.82 | 121 | empty |
| 4 | 1064 | 0.81 | 0.82 | 134 | empty |
| 5 | 1088 | 0.81 | 0.82 | 133 | empty |
Interfaces
25 interfaces between chains.
- N–H · 369 Ų buried · 3 hydrogen bonds · protein-protein
- M–G · 367 Ų buried · 2 hydrogen bonds · protein-protein
- I–C · 358 Ų buried · 2 hydrogen bonds · protein-protein
- K–E · 354 Ų buried · 1 hydrogen bond · protein-protein
- J–D · 346 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6BNW · CryoEM structure of Myosin VI-Actin complex in the ADP state, backbone-averaged with side… · the same entry in another collection · chain J against J, 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
- Every structure of UniProt P68135
- Elsewhere: RCSB PDB 6BNW · PDBe 6BNW · UniProt F1RQI7 · UniProt P68135
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