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Human picobirnavirus ht-cp vlp

Analyse Human picobirnavirus ht-cp vlp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6Z8E
Type
protein
Length
1,018 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein precursor
UniProt
Q50LE5
Pockets
12 · best druggability 0.70

Structure

electron microscopy · 2 distinct chains · 34% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACapsid protein precursorprotein50634% helix, 19% strandQ50LE5
BCapsid protein precursorprotein51235% helix, 20% strandQ50LE5

Pockets

12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12750.700.8534empty
2610.580.9020empty
31400.530.8122empty
42520.520.7644empty
52210.480.7542empty

Interfaces

1 interface between chains.

  • A–B · 5601 Ų buried · 75 hydrogen bonds · protein-protein

Compared structures

  • 6Z8E · Human Picobirnavirus Ht-CP VLP · the same entry in another collection · chain A against A, TM-score 1.00

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