Research workbench
Motor domain of myoe, a class-I myosin
Analyse Motor domain of myoe, a class-I myosin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LKX
- Type
- protein
- Length
- 2,639 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin ie heavy chain
- UniProt
- Q03479
- Ligands
- ADP, MG, VO4
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 4 distinct chains · 49% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin ie heavy chain | protein | 650 | 50% helix, 13% strand | Q03479 |
| B | Myosin ie heavy chain | protein | 650 | 48% helix, 12% strand | Q03479 |
| C | Myosin ie heavy chain | protein | 679 | 49% helix, 12% strand | Q03479 |
| D | Myosin ie heavy chain | protein | 660 | 51% helix, 12% strand | Q03479 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- VO4 · Vanadate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1075 | 0.82 | 0.83 | 79 | empty |
| 2 | 1191 | 0.81 | 0.82 | 86 | empty |
| 3 | 1088 | 0.75 | 0.77 | 72 | empty |
| 4 | 623 | 0.71 | 0.79 | 60 | empty |
| 5 | 721 | 0.70 | 0.77 | 67 | empty |
Interfaces
3 interfaces between chains.
- A–C · 906 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 832 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 513 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
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 Q03479
- Elsewhere: RCSB PDB 1LKX · PDBe 1LKX · UniProt Q03479
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.