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The asymmetric-reconstructed cryo-EM structure of zika virus-FABZK2B10 complex

Analyse The asymmetric-reconstructed cryo-EM structure of zika virus-FABZK2B10 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6JFH
Type
protein
Length
3,075 residues
Chains
12
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Zikv structural E protein; Strutural protein M; FABZK2B10 heavy chain; FABZK2B10 light…
EC
3.4.21.91, 3.6.1.15, 3.6.4.13, 2.1.1.56, 2.1.1.57, 2.7.7.48
UniProt
A0A024B7W1
Pockets
8 · best druggability 0.42

Structure

electron microscopy · 4 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, EZikv structural E proteinprotein5010% helix, 0% strand—
B, D, FStrutural protein M (EC 3.4.21.91, 3.6.1.15, 3.6.4.13, 2.1.1.56, 2.1.1.57, 2.7.7.48)protein750% helix, 0% strandA0A024B7W1
H, K, MFABZK2B10 heavy chainprotein2350% helix, 0% strand—
L, I, NFABZK2B10 light chainprotein2140% helix, 0% strand—

Pockets

8 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11290.420.7435empty
21260.410.7336empty
31270.390.7233empty
4910.350.7322empty
5930.340.7226empty

Interfaces

16 interfaces between chains.

  • A–B · 251 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 234 Ų buried · 0 hydrogen bonds · protein-protein
  • C–E · 229 Ų buried · 0 hydrogen bonds · protein-protein
  • E–F · 225 Ų buried · 0 hydrogen bonds · protein-protein
  • D–F · 141 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6JFH · The asymmetric-reconstructed cryo-EM structure of Zika virus-FabZK2B10 complex · the same entry in another collection · chain A against A, TM-score 1.00

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