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Cryoem structure of myosinvi-actin complex in the rigor (nucleotide- free) state, backbone-averaged with side chains truncated to alanine
Analyse Cryoem structure of myosinvi-actin complex in the rigor (nucleotide- free)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BNV
- Type
- protein
- Length
- 8,588 residues
- Chains
- 20
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Unconventional myosin-VI; Actin, alpha skeletal muscle; Calmodulin
- UniProt
- F1RQI7, P68135, P62149
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 3 distinct chains · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| I, J, K, L, M, N | Unconventional myosin-VI | protein | 797 | 46% helix, 16% strand | F1RQI7 |
| A, B, C, D, E, F, G, H | Actin, alpha skeletal muscle | protein | 367 | 41% helix, 19% strand | P68135 |
| O, P, Q, R, S, T | Calmodulin | protein | 145 | 61% helix, 6% strand | P62149 |
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 | 981 | 0.83 | 0.84 | 158 | empty |
| 2 | 1198 | 0.81 | 0.82 | 150 | empty |
| 3 | 762 | 0.81 | 0.84 | 117 | empty |
| 4 | 771 | 0.81 | 0.84 | 115 | empty |
| 5 | 1142 | 0.80 | 0.82 | 135 | empty |
Interfaces
31 interfaces between chains.
- I–O · 593 Ų buried · 0 hydrogen bonds · protein-protein
- M–S · 578 Ų buried · 0 hydrogen bonds · protein-protein
- J–P · 572 Ų buried · 0 hydrogen bonds · protein-protein
- N–T · 566 Ų buried · 0 hydrogen bonds · protein-protein
- L–R · 560 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6BNV · CryoEM structure of MyosinVI-actin complex in the rigor (nucleotide-free) state… · the same entry in another collection · chain Q against Q, 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
- Every structure of UniProt P62149
- Elsewhere: RCSB PDB 6BNV · PDBe 6BNV · UniProt F1RQI7 · UniProt P68135 · UniProt P62149
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