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Interleukin-2 mutant D10

Analyse Interleukin-2 mutant D10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3QB1
Type
protein
Length
947 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Interleukin-2
UniProt
P60568
Pockets
9 · best druggability 0.72

Structure

x-ray diffraction · 6 distinct chains · 68% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, FInterleukin-2protein12468% helix, 8% strandP60568
CInterleukin-2protein11968% helix, 8% strandP60568
DInterleukin-2protein11068% helix, 9% strandP60568
EInterleukin-2protein11766% helix, 9% strandP60568
GInterleukin-2protein11168% helix, 9% strandP60568
HInterleukin-2protein11869% helix, 8% strandP60568

Pockets

9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111810.720.7695empty
23670.640.7943empty
34200.620.7734empty
42600.570.7823empty
52780.540.7623empty

Interfaces

9 interfaces between chains.

  • A–B · 857 Ų buried · 9 hydrogen bonds · protein-protein
  • C–F · 560 Ų buried · 8 hydrogen bonds · protein-protein
  • A–H · 497 Ų buried · 4 hydrogen bonds · protein-protein
  • C–E · 480 Ų buried · 6 hydrogen bonds · protein-protein
  • C–D · 212 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

  • 3QB1 · Interleukin-2 mutant D10 · the same entry in another collection · chain H against H, TM-score 1.00
  • P60568 · AlphaFold monomer V2.0 prediction for interleukin-2 (P60568) · a predicted model of the same protein · chain D against A, TM-score 0.97

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