Research workbench
Crystal structure of the mgatp complex for the motor domain of dictyostelium myosin II
Analyse Crystal structure of the mgatp complex for the motor domain of dictyostelium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FMW
- Type
- protein
- Length
- 738 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin II heavy chain
- UniProt
- P08799
- Ligands
- ATP, MG
- Pockets
- 7 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin II heavy chain | protein | 738 | 46% helix, 15% strand | P08799 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1179 | 0.83 | 0.84 | 116 | MG, ATP |
| 2 | 1027 | 0.73 | 0.76 | 75 | empty |
| 3 | 75 | 0.64 | 0.91 | 25 | empty |
| 4 | 119 | 0.53 | 0.82 | 19 | empty |
| 5 | 72 | 0.41 | 0.80 | 14 | empty |
Compared structures
- 1FMW · Crystal structure of the mgatp complex for the motor domain of dictyostelium myosin II · 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 0.89
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 1FMW · PDBe 1FMW · UniProt P08799
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