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Crystal Structure of Quaternary-Specific RSV-Neutralizing Human Antibody AM14

Analyse Crystal Structure of Quaternary-Specific RSV-Neutralizing Human Antibody AM14 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ZYK
Type
protein
Length
858 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Source
Homo sapiens
Molecule
AM14 Fab heavy chain; AM14 light chain
Ligands
SO4
Pockets
8 · best druggability 0.66

Structure

x-ray diffraction · resolution 2 · 4 distinct chains · 7% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
HAM14 Fab heavy chainprotein2148% helix, 52% strand—
LAM14 light chainprotein2135% helix, 51% strand—
AAM14 Fab heavy chainprotein2177% helix, 53% strand—
BAM14 light chainprotein2146% helix, 50% strand—

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains H, L, B
  • EDO · 1,2-ethanediol · additive · 5 copies · chains H, L, A, B
  • ACT · Acetate ion · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14260.660.7954empty
25040.640.7741SO4
31950.570.8033empty
4640.540.8822EDO
51610.440.7521empty

Interfaces

3 interfaces between chains.

  • H–L · 1778 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 1775 Ų buried · 13 hydrogen bonds · protein-protein
  • L–B · 902 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 4ZYK · Crystal structure of quaternary-specific rsv-neutralizing human antibody AM14 · the same entry in another collection · chain A against A, TM-score 1.00

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