Research workbench
Structure of myosin viia MYTH4-ferm-SH3 in complex with the CEN1 of sans
Analyse Structure of myosin viia MYTH4-ferm-SH3 in complex with the CEN1 of sans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PVL
- Type
- protein
- Length
- 613 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin viia isoform 1; Usher syndrome type-1G protein
- UniProt
- Q5MJ57, Q495M9
- Ligands
- PO4
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin viia isoform 1 | protein | 597 | 44% helix, 17% strand | Q5MJ57 |
| B | Usher syndrome type-1G protein | protein | 16 | 0% helix, 31% strand | Q495M9 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · 9 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 375 | 0.65 | 0.79 | 42 | empty |
| 2 | 83 | 0.48 | 0.82 | 16 | empty |
| 3 | 69 | 0.42 | 0.80 | 17 | empty |
| 4 | 71 | 0.38 | 0.78 | 23 | empty |
| 5 | 70 | 0.27 | 0.72 | 19 | GOL |
Interfaces
1 interface between chains.
- A–B · 1189 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 3PVL · Structure of myosin VIIa MyTH4-FERM-SH3 in complex with the CEN1 of Sans · the same entry in another collection · chain A against A, TM-score 1.00
- Q495M9 · AlphaFold monomer V2.0 prediction for usher syndrome type-1G protein (Q495M9) · a predicted model of the same protein · chain B against A, TM-score 0.21
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 Q5MJ57
- Every structure of UniProt Q495M9
- Elsewhere: RCSB PDB 3PVL · PDBe 3PVL · UniProt Q5MJ57 · UniProt Q495M9
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