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AAV8 baculovirus-SF9 produced, empty capsid

Analyse AAV8 baculovirus-SF9 produced, empty capsid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6UBM
Type
protein
Length
519 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein
UniProt
Q8JQF8
Pockets
8 · best druggability 0.50

Structure

electron microscopy · 1 distinct chain · 6% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapsid proteinprotein5196% helix, 32% strandQ8JQF8

Pockets

8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12720.500.7425empty
21460.480.7719empty
3810.410.7921empty
41290.410.7524empty
51480.400.7324empty

Compared structures

  • 6UBM · AAV8 Baculovirus-Sf9 produced, empty capsid · the same entry in another collection · chain A against A, TM-score 1.00

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