Research workbench
Myosin
Analyse Myosin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1BR1
- Type
- protein
- Length
- 3,740 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin
- EC
- 3.6.1.32
- UniProt
- P10587, P02607
- Ligands
- ALF, ADP, MG
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G | Myosin (EC 3.6.1.32) | protein | 787 | 42% helix, 13% strand | P10587 |
| B, D, F, H | Myosin (EC 3.6.1.32) | protein | 148 | 52% helix, 3% strand | P02607 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · 4 copies · chains A, C, E, G
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, C, E, G
- MG · Magnesium ion · metal · 4 copies · chains A, C, E, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 909 | 0.79 | 0.82 | 67 | empty |
| 2 | 1078 | 0.78 | 0.80 | 72 | empty |
| 3 | 1045 | 0.78 | 0.80 | 79 | empty |
| 4 | 1045 | 0.78 | 0.80 | 67 | empty |
| 5 | 764 | 0.77 | 0.81 | 66 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2177 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 2167 Ų buried · 21 hydrogen bonds · protein-protein
- E–F · 2146 Ų buried · 21 hydrogen bonds · protein-protein
- G–H · 2093 Ų buried · 18 hydrogen bonds · protein-protein
- A–H · 416 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1BR1 · Smooth muscle myosin motor domain-essential light chain complex with MGADP.ALF4 bound at… · the same entry in another collection · chain H against H, TM-score 1.00
- P10587 · AlphaFold monomer V2.0 prediction for myosin-11 (P10587) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P02607 · AlphaFold monomer V2.0 prediction for myosin light polypeptide 6 (P02607) · a predicted model of the same protein · chain B against A, TM-score 0.96
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 P10587
- Every structure of UniProt P02607
- Elsewhere: RCSB PDB 1BR1 · PDBe 1BR1 · UniProt P10587 · UniProt P02607
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