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Cryo-EM structure of hepatitis B virus T=3 capsid in complex with the fluorescent allosteric modulator hap-tamra

Analyse Cryo-EM structure of hepatitis B virus T=3 capsid in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BVN
Type
protein
Length
432 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Capsid protein
UniProt
P03147
Ligands
E9D
Pockets
3 · best druggability 0.71

Structure

electron microscopy · 1 distinct chain · 68% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
C, B, ACapsid proteinprotein14468% helix, 0% strandP03147

Ligands and binding sites

  • E9D · Heteroaryldihydropyrimidine tetramethylrodamine · ligand · chains C, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13480.710.8334E9D
22560.660.8337empty
3620.350.7716empty

Interfaces

3 interfaces between chains.

  • B–A · 1966 Ų buried · 13 hydrogen bonds · protein-protein
  • C–B · 510 Ų buried · 2 hydrogen bonds · protein-protein
  • C–A · 16 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6BVN · Cryo-EM Structure of Hepatitis B virus T=3 capsid in complex with the fluorescent… · the same entry in another collection · chain C against C, TM-score 1.00

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