Research workbench
Rigor-like structures of muscle myosins reveal key mechanical elements in the transduction pathways of this allosteric motor
Analyse Rigor-like structures of muscle myosins reveal key mechanical elements in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OS8
- Type
- protein
- Length
- 1,088 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin heavy chain; Myosin regulatory light chain; Myosin essential light chain
- UniProt
- Q26080, Q26068, Q26066
- Ligands
- MG, CA
- Pockets
- 15 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 44% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin heavy chain | protein | 798 | 45% helix, 12% strand | Q26080 |
| B | Myosin regulatory light chain | protein | 135 | 36% helix, 4% strand | Q26068 |
| C | Myosin essential light chain | protein | 155 | 49% helix, 7% strand | Q26066 |
Ligands and binding sites
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 | 1000 | 0.82 | 0.83 | 137 | empty |
| 2 | 186 | 0.76 | 0.92 | 33 | empty |
| 3 | 151 | 0.76 | 0.93 | 28 | empty |
| 4 | 296 | 0.76 | 0.87 | 50 | empty |
| 5 | 551 | 0.73 | 0.81 | 56 | empty |
Interfaces
3 interfaces between chains.
- A–C · 2153 Ų buried · 18 hydrogen bonds · protein-protein
- A–B · 1813 Ų buried · 16 hydrogen bonds · protein-protein
- B–C · 246 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2OS8 · Rigor-like structures of muscle myosins reveal key mechanical elements in the… · 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 Q26080
- Every structure of UniProt Q26068
- Every structure of UniProt Q26066
- Elsewhere: RCSB PDB 2OS8 · PDBe 2OS8 · UniProt Q26080 · UniProt Q26068 · UniProt Q26066
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