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Molecular dynamics flexible fitting model of coxsackievirus A16 empty procapsid VP3 subunit

Analyse Molecular dynamics flexible fitting model of coxsackievirus A16 empty procapsid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5TSL
Type
protein
Length
229 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coxsackievirus A16
Pockets
1 · best druggability 0.53

Structure

electron microscopy · 1 distinct chain · 10% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CCoxsackievirus A16protein22910% helix, 31% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11780.530.7925empty

Compared structures

  • 5TSL · Molecular Dynamics Flexible Fitting Model of Coxsackievirus A16 empty Procapsid VP3… · the same entry in another collection · chain C against C, TM-score 1.00

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