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The crystal structure of the interleukin 11 alpha receptor

Analyse The crystal structure of the interleukin 11 alpha receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6O4P
Type
protein
Length
580 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Interleukin-11 receptor subunit alpha
UniProt
Q14626
Ligands
NAG, BMA, MAN, SO4
Pockets
2 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInterleukin-11 receptor subunit alphaprotein2951% helix, 43% strandQ14626
BInterleukin-11 receptor subunit alphaprotein2851% helix, 46% strandQ14626

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar
  • MAN · alpha-D-mannopyranose · sugar
  • SO4 · Sulfate ion · ion · 11 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1790.730.9625empty
21490.430.7520SO4

Interfaces

1 interface between chains.

  • A–B · 1098 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

  • 6O4P · The crystal structure of the interleukin 11 alpha receptor · the same entry in another collection · chain A against A, TM-score 1.00
  • Q14626 · AlphaFold monomer V2.0 prediction for interleukin-11 receptor subunit alpha (Q14626) · a predicted model of the same protein · chain A against A, TM-score 0.96

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