Research workbench
Placopecten striated muscle myosin II
Analyse Placopecten striated muscle myosin II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EC6
- Type
- protein
- Length
- 1,083 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin heavy chain; Myosin regulatory light chain; Myosin essential light chain
- UniProt
- Q26079, Q26069, Q26066
- Ligands
- CA
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 30% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin heavy chain | protein | 802 | 28% helix, 4% strand | Q26079 |
| B | Myosin regulatory light chain | protein | 126 | 27% helix, 5% strand | Q26069 |
| C | Myosin essential light chain | protein | 155 | 41% helix, 6% strand | Q26066 |
Ligands and binding sites
- CA · Calcium ion · metal · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 950 | 0.81 | 0.83 | 111 | empty |
| 2 | 172 | 0.80 | 0.95 | 38 | empty |
| 3 | 883 | 0.79 | 0.82 | 82 | empty |
| 4 | 405 | 0.79 | 0.87 | 46 | empty |
| 5 | 688 | 0.78 | 0.83 | 84 | empty |
Interfaces
3 interfaces between chains.
- A–C · 2126 Ų buried · 22 hydrogen bonds · protein-protein
- A–B · 1605 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 244 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2EC6 · Placopecten Striated Muscle Myosin II · the same entry in another collection · chain A against A, TM-score 1.00
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 Q26079
- Every structure of UniProt Q26069
- Every structure of UniProt Q26066
- Elsewhere: RCSB PDB 2EC6 · PDBe 2EC6 · UniProt Q26079 · UniProt Q26069 · UniProt Q26066
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