Research workbench
Structure of the C-terminally extended domain MY4 of human myomesin (space group P21)
Analyse Structure of the C-terminally extended domain MY4 of human myomesin (space… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FM4
- Type
- protein
- Length
- 617 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myomesin-1
- UniProt
- P52179
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 3 distinct chains · 2% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, E, F | Myomesin-1 | protein | 101 | 0% helix, 44% strand | P52179 |
| B | Myomesin-1 | protein | 108 | 6% helix, 41% strand | P52179 |
| C | Myomesin-1 | protein | 105 | 0% helix, 40% strand | P52179 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 915 | 0.83 | 0.84 | 102 | empty |
| 2 | 225 | 0.56 | 0.78 | 28 | empty |
| 3 | 78 | 0.29 | 0.72 | 15 | empty |
Interfaces
8 interfaces between chains.
- A–B · 717 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 707 Ų buried · 5 hydrogen bonds · protein-protein
- E–F · 625 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 615 Ų buried · 6 hydrogen bonds · protein-protein
- D–E · 432 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 5FM4 · Structure of the C-terminally extended domain My4 of human myomesin (space group P21) · the same entry in another collection · chain F against F, TM-score 1.00
- P52179 · AlphaFold monomer V2.0 prediction for myomesin-1 (P52179) · a predicted model of the same protein · chain A 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 P52179
- Elsewhere: RCSB PDB 5FM4 · PDBe 5FM4 · UniProt P52179
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