Research workbench
Crystal structure of myosin-XI motor domain in complex with ADP-ALF4
Analyse Crystal structure of myosin-XI motor domain in complex with ADP-ALF4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7DHW
- Type
- protein
- Length
- 726 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Motor domain of myosin
- UniProt
- Q9LKB9
- Ligands
- ALF, ADP, MG
- Pockets
- 6 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Motor domain of myosin | protein | 726 | 45% helix, 17% strand | Q9LKB9 |
Ligands and binding sites
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
- GOL · Glycerol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 653 | 0.72 | 0.79 | 69 | MG, GOL |
| 2 | 533 | 0.68 | 0.78 | 57 | MG, ALF, ADP, GOL |
| 3 | 609 | 0.67 | 0.77 | 51 | empty |
| 4 | 117 | 0.63 | 0.88 | 30 | empty |
| 5 | 132 | 0.53 | 0.81 | 27 | 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 Q9LKB9
- Elsewhere: RCSB PDB 7DHW · PDBe 7DHW · UniProt Q9LKB9
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