MolNFT v1 · #144693 · protein
High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing
6C1G · Unconventional myosin-ib: “High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing”. Electron microscopy, 2 ligands (ADP, MG), 20 pockets (best druggability 0.81). MolNFT v1…
- PDB
- 6C1G
- Type
- protein
- Length
- 2,752 residues
- Chains
- 7
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Unconventional myosin-ib; Calmodulin; Actin, alpha skeletal muscle
- UniProt
- Q05096, P68135
- Ligands
- ADP, MG
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 3 distinct chains · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| P | Unconventional myosin-ib | protein | 729 | 47% helix, 12% strand | Q05096 |
| R | Calmodulin | protein | 148 | 52% helix, 4% strand | — |
| A, B, C, D, E | Actin, alpha skeletal muscle | protein | 375 | 41% helix, 19% strand | P68135 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains P, A, B, C, D, E
- MG · Magnesium ion · metal · 6 copies · chains P, A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1057 | 0.81 | 0.82 | 90 | empty |
| 2 | 942 | 0.79 | 0.81 | 69 | empty |
| 3 | 730 | 0.77 | 0.82 | 64 | empty |
| 4 | 1183 | 0.76 | 0.79 | 114 | empty |
| 5 | 380 | 0.71 | 0.83 | 40 | empty |
Interfaces
10 interfaces between chains.
- P–B · 1356 Ų buried · 15 hydrogen bonds · protein-protein
- A–C · 1328 Ų buried · 15 hydrogen bonds · protein-protein
- B–D · 1317 Ų buried · 15 hydrogen bonds · protein-protein
- C–E · 1317 Ų buried · 15 hydrogen bonds · protein-protein
- P–D · 610 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 6C1G · High-Resolution Cryo-EM Structures of Actin-bound Myosin States Reveal the Mechanism of… · the same entry in another collection · chain E against E, TM-score 1.00
- Q05096 · AlphaFold monomer V2.0 prediction for unconventional myosin-ib (Q05096) · a predicted model of the same protein · chain P against A, TM-score 0.98
- P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain D against A, TM-score 0.95
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 Q05096
- Every structure of UniProt P68135
- Elsewhere: RCSB PDB 6C1G · PDBe 6C1G · UniProt Q05096 · UniProt P68135
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