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Zika specific antibody, zv-64, bound to zika envelope diii

Analyse Zika specific antibody, zv-64, bound to zika envelope diii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5KVF
Type
protein
Length
546 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Zika envelope diii; Zv-64 antibody Fab light chain; Zv-64 antibody Fab heavy chain
UniProt
A0A024B7W1
Pockets
6 · best druggability 0.68

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
EZika envelope diiiprotein1053% helix, 45% strandA0A024B7W1
LZv-64 antibody Fab light chainprotein2206% helix, 55% strand—
HZv-64 antibody Fab heavy chainprotein2218% helix, 50% strand—

Ligands and binding sites

  • GOL · Glycerol · additive · 5 copies · chains E, H

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18120.680.7565GOL
21080.410.7619empty
31240.410.7525empty
4910.350.7423empty
5510.320.7719empty

Interfaces

3 interfaces between chains.

  • L–H · 2046 Ų buried · 21 hydrogen bonds · protein-protein
  • E–L · 542 Ų buried · 9 hydrogen bonds · protein-protein
  • E–H · 366 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 1 modified (disulfide, cyclization).

Compared structures

  • 5KVF · Zika specific antibody, ZV-64, bound to ZIKA envelope DIII · the same entry in another collection · chain E against E, TM-score 1.00

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