Research workbench
Insights into the importance of hydrogen bonding in the gamma- phosphate binding pocket of myosin: structural and functional studies of SER236
Analyse Insights into the importance of hydrogen bonding in the gamma- phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MYH
- Type
- protein
- Length
- 708 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin-2 heavy chain
- UniProt
- P08799
- Ligands
- ADP, BIT, MG, VO4
- Pockets
- 8 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Myosin-2 heavy chain | protein | 708 | 46% helix, 17% strand | P08799 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains X
- BIT · (-)-1-phenyl-1,2,3,4-tetrahydro-4-hydroxypyrrolo[2,3-B]-7-methylquinolin-4-one · ligand · chains X
- MG · Magnesium ion · metal · chains X
- VO4 · Vanadate ion · ion · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1032 | 0.80 | 0.81 | 93 | BIT |
| 2 | 421 | 0.68 | 0.80 | 64 | MG, VO4, ADP |
| 3 | 282 | 0.55 | 0.76 | 27 | empty |
| 4 | 86 | 0.48 | 0.82 | 21 | empty |
| 5 | 64 | 0.39 | 0.79 | 13 | empty |
Compared structures
- 3MYH · Insights into the Importance of Hydrogen Bonding in the Gamma-Phosphate Binding Pocket of… · the same entry in another collection · chain X against X, TM-score 1.00
- P08799 · AlphaFold monomer V2.0 prediction for myosin-2 heavy chain (P08799) · a predicted model of the same protein · chain X against A, TM-score 0.97
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 3MYH · PDBe 3MYH · UniProt P08799
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