Research workbench
Mutant myosin-II-ggg motor domain
Analyse Mutant myosin-II-ggg motor domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7B19
- Type
- protein
- Length
- 750 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin-2 heavy CHAIN,MYOSIN-2 heavy chain
- UniProt
- P08799
- Ligands
- AD9, GLC, MG
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin-2 heavy CHAIN,MYOSIN-2 heavy chain | protein | 750 | 46% helix, 16% strand | P08799 |
Ligands and binding sites
- AD9 · Adp metavanadate · ligand · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 6 copies · chains A
- MLI · Malonate ion · additive · 5 copies · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 916 | 0.78 | 0.81 | 75 | PEG, GOL, MLI |
| 2 | 501 | 0.68 | 0.79 | 55 | AD9, MG, MLI |
| 3 | 663 | 0.68 | 0.76 | 54 | empty |
| 4 | 80 | 0.47 | 0.82 | 26 | GOL |
| 5 | 60 | 0.36 | 0.78 | 14 | empty |
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 P08799
- Elsewhere: RCSB PDB 7B19 · PDBe 7B19 · UniProt P08799
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