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Structure of the C-type lectin domain of CD23

Analyse Structure of the C-type lectin domain of CD23 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1T8D
Type
protein
Length
143 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Low affinity immunoglobulin epsilon Fc receptor
UniProt
P06734
Pockets
1 · best druggability 0.38

Structure

solution nmr · 1 distinct chain · 15% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALow affinity immunoglobulin epsilon Fc receptorprotein14315% helix, 27% strandP06734

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11240.380.7425empty

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 1T8D · Structure of the C-type lectin domain of CD23 · the same entry in another collection · chain A against A, TM-score 1.00
  • P06734 · AlphaFold monomer V2.0 prediction for low affinity immunoglobulin epsilon Fc receptor… · a predicted model of the same protein · chain A against A, TM-score 0.71

Analyse

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