Research workbench
Structure of the human myosin-X MYTH4-ferm cassette bound to its specific cargo, dcc
Analyse Structure of the human myosin-X MYTH4-ferm cassette bound to its specific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AU4
- Type
- protein
- Length
- 556 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin-X; Netrin receptor dcc
- UniProt
- Q9HD67, P43146
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Myosin-X | protein | 524 | 46% helix, 16% strand | Q9HD67 |
| B | Netrin receptor dcc | protein | 32 | 81% helix, 0% strand | P43146 |
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 | 337 | 0.74 | 0.86 | 43 | empty |
| 2 | 280 | 0.54 | 0.76 | 34 | empty |
| 3 | 233 | 0.52 | 0.76 | 39 | empty |
| 4 | 150 | 0.47 | 0.77 | 26 | empty |
| 5 | 55 | 0.38 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 862 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 3AU4 · Structure of the human myosin-X MyTH4-FERM cassette bound to its specific cargo, DCC · the same entry in another collection · chain A against A, TM-score 1.00
- Q9HD67 · AlphaFold monomer V2.0 prediction for unconventional myosin-X (Q9HD67) · a predicted model of the same protein · chain A against A, TM-score 0.92
- P43146 · AlphaFold monomer V2.0 prediction for netrin receptor dcc (P43146) · a predicted model of the same protein · chain B against A, TM-score 0.55
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 Q9HD67
- Every structure of UniProt P43146
- Elsewhere: RCSB PDB 3AU4 · PDBe 3AU4 · UniProt Q9HD67 · UniProt P43146
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