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Crystal structure of human interleukin-5 in complex with its alpha receptor

Analyse Crystal structure of human interleukin-5 in complex with its alpha receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3VA2
Type
protein
Length
523 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Interleukin-5; Interleukin-5 receptor subunit alpha
UniProt
P05113, Q01344
Pockets
4 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 27% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInterleukin-5protein10766% helix, 6% strandP05113
BInterleukin-5protein10959% helix, 5% strandP05113
CInterleukin-5 receptor subunit alphaprotein3072% helix, 52% strandQ01344

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17510.750.8060empty
24200.700.8145empty
3950.660.9120empty
41070.430.7819empty

Interfaces

3 interfaces between chains.

  • A–B · 3428 Ų buried · 23 hydrogen bonds · protein-protein
  • A–C · 879 Ų buried · 22 hydrogen bonds · protein-protein
  • B–C · 479 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide (disulfide).

Compared structures

  • 3VA2 · Crystal structure of human Interleukin-5 in complex with its alpha receptor · 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 C against A, TM-score 0.99
  • P05113 · AlphaFold monomer V2.0 prediction for interleukin-5 (P05113) · a predicted model of the same protein · chain B against A, TM-score 0.97

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