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Structure of the complex of the IL-5 inhibitory peptide AF17121 bound to the IL-5 receptor IL-5Ralpha

Analyse Structure of the complex of the IL-5 inhibitory peptide AF17121 bound to the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6H41
Type
protein
Length
327 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.75
Source
Homo sapiens; SYNTHETIC CONSTRUCT
Molecule
Interleukin-5 receptor subunit alpha; Val-asp-glu-cys-TRP-arg-ile-ile-ala-ser-his-thr-TRP…
UniProt
Q01344
Pockets
1 · best druggability 0.31

Structure

x-ray diffraction · resolution 2.75 · 2 distinct chains · 2% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInterleukin-5 receptor subunit alphaprotein3092% helix, 51% strandQ01344
BVal-asp-glu-cys-TRP-arg-ile-ile-ala-ser-his-thr-TRP-phe-cys-ala-glu-gluprotein180% helix, 33% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1680.310.7415empty

Interfaces

1 interface between chains.

  • A–B · 921 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 6H41 · Structure of the complex of the il-5 inhibitory peptide AF17121 bound to the il-5… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q01344 · AlphaFold monomer V2.0 prediction for interleukin-5 receptor subunit alpha (Q01344) · a predicted model of the same protein · chain A against A, TM-score 0.97

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