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AlphaFold monomer V2.0 prediction for interleukin-12 subunit alpha (P43431)

Analyse AlphaFold monomer V2.0 prediction for interleukin-12 subunit alpha (P43431) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
P43431
Type
protein
Length
215 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x9aD208242de9c7C25e2FbA3404A2bA0A5f6c2Eac
Molecule
Interleukin-12 subunit alpha
UniProt
P43431
Pockets
2 · best druggability 0.41

Structure

1 distinct chain · 60% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInterleukin-12 subunit alphaprotein21560% helix, 0% strandP43431

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11000.410.7721empty
2770.360.7616empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 8CR6 · mouse Interleukin-12 · an experimental structure of the same protein · chain A against B, TM-score 0.73
  • 8ODZ · Cryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling… · an experimental structure of the same protein · chain A against A, TM-score 0.70
  • 8PB1 · Cryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling… · an experimental structure of the same protein · chain A against A, TM-score 0.69
  • 8OE0 · Cryo-EM structure of a pre-dimerized murine IL-12 complete extracellular signaling… · an experimental structure of the same protein · chain A against A, TM-score 0.68

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