Research workbench
Truncated head of myosin from dictyostelium discoideum complexed with mgadp-ALF4
Analyse Truncated head of myosin from dictyostelium discoideum complexed with mgadp-ALF4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1MND
- Type
- protein
- Length
- 641 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin
- EC
- 3.6.1.32
- UniProt
- P08799
- Ligands
- ALF, ADP, MG
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin (EC 3.6.1.32) | protein | 641 | 43% helix, 15% strand | P08799 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 844 | 0.75 | 0.79 | 73 | empty |
| 2 | 378 | 0.64 | 0.79 | 52 | ALF, ADP |
| 3 | 150 | 0.63 | 0.86 | 27 | empty |
| 4 | 100 | 0.46 | 0.79 | 19 | empty |
| 5 | 52 | 0.29 | 0.75 | 14 | empty |
Compared structures
- 1MND · Truncated head of myosin from dictyostelium discoideum complexed with mgadp-ALF4 · the same entry in another collection · chain A against A, TM-score 1.00
- P08799 · AlphaFold monomer V2.0 prediction for myosin-2 heavy chain (P08799) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P08799
- Elsewhere: RCSB PDB 1MND · PDBe 1MND · UniProt P08799
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