Research workbench
Adeno-associated virus (aav-dj) - cryo-EM structure at 1.56 ångström resolution
Analyse Adeno-associated virus (aav-dj) - cryo-EM structure at 1.56 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7KFR
- Type
- protein
- Length
- 521 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein VP1
- UniProt
- Q6JC41
- Ligands
- MG
- Pockets
- 6 · best druggability 0.71
Structure
electron microscopy · 1 distinct chain · 8% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Capsid protein VP1 | protein | 521 | 8% helix, 34% strand | Q6JC41 |
Ligands and binding sites
- MG · Magnesium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 921 | 0.71 | 0.75 | 95 | empty |
| 2 | 118 | 0.45 | 0.78 | 26 | empty |
| 3 | 134 | 0.40 | 0.74 | 23 | empty |
| 4 | 118 | 0.39 | 0.74 | 18 | empty |
| 5 | 68 | 0.33 | 0.76 | 19 | empty |
Compared structures
- 7KFR · Adeno-Associated Virus (AAV-DJ) - cryo-EM structure at 1.56 Angstrom Resolution · 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 Q6JC41
- Elsewhere: RCSB PDB 7KFR · PDBe 7KFR · UniProt Q6JC41
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