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D2 domain of human IFNAR2

Analyse D2 domain of human IFNAR2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3S8W
Type
protein
Length
250 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Interferon ALPHA/BETA receptor 2
UniProt
P48551
Ligands
CL
Pockets
1 · best druggability 0.62

Structure

x-ray diffraction · 3 distinct chains · 0% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AInterferon ALPHA/BETA receptor 2protein770% helix, 51% strandP48551
BInterferon ALPHA/BETA receptor 2protein810% helix, 54% strandP48551
CInterferon ALPHA/BETA receptor 2protein920% helix, 52% strandP48551

Ligands and binding sites

  • CL · Chloride ion · ion · 2 copies · chains A, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14970.620.7570empty

Interfaces

3 interfaces between chains.

  • A–C · 589 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 359 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 120 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified, 3 disulfide (engineered, disulfide).

Compared structures

  • 3S8W · D2 domain of human IFNAR2 · the same entry in another collection · chain A against A, TM-score 1.00
  • P48551 · AlphaFold monomer V2.0 prediction for interferon ALPHA/BETA receptor 2 (P48551) · a predicted model of the same protein · chain B against A, TM-score 0.96

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