Research workbench
Structure of the two-fold capsomer of the DARC2 capsid
Analyse Structure of the two-fold capsomer of the DARC2 capsid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TAU
- Type
- protein
- Length
- 984 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Activity-regulated cytoskeleton associated protein 2
- UniProt
- Q7JV70
- Pockets
- 20 · best druggability 0.71
Structure
electron microscopy · 1 distinct chain · 57% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Activity-regulated cytoskeleton associated protein 2 | protein | 164 | 57% helix, 1% strand | Q7JV70 |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 637 | 0.71 | 0.79 | 77 | empty |
| 2 | 662 | 0.71 | 0.78 | 75 | empty |
| 3 | 352 | 0.63 | 0.79 | 52 | empty |
| 4 | 364 | 0.61 | 0.77 | 50 | empty |
| 5 | 132 | 0.61 | 0.85 | 27 | empty |
Interfaces
6 interfaces between chains.
- B–F · 1085 Ų buried · 7 hydrogen bonds · protein-protein
- C–E · 1069 Ų buried · 7 hydrogen bonds · protein-protein
- D–E · 1055 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 1049 Ų buried · 0 hydrogen bonds · protein-protein
- D–F · 939 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 6TAU · Structure of the two-fold capsomer of the dArc2 capsid · the same entry in another collection · chain F against F, TM-score 1.00
- Q7JV70 · AlphaFold monomer V2.0 prediction for activity-regulated cytoskeleton associated protein… · a predicted model of the same protein · chain C against A, TM-score 0.92
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 Q7JV70
- Elsewhere: RCSB PDB 6TAU · PDBe 6TAU · UniProt Q7JV70
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