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Crystal structure analysis of the human IgE-Fc CEPSILON3- CEPSILON4 fragment.

Analyse Crystal structure analysis of the human IgE-Fc CEPSILON3- CEPSILON4 fragment. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FP5
Type
protein
Length
208 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
IgE heavy chain epsilon-1
UniProt
P01854
Pockets
2 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AIgE heavy chain epsilon-1protein20811% helix, 47% strandP01854

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1770.550.8617empty
21110.350.7322empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 1FP5 · Crystal structure analysis of the human IgE-Fc CEPSILON3-CEPSILON4 fragment. · the same entry in another collection · chain A against A, TM-score 1.00
  • P01854 · AlphaFold monomer V2.0 prediction for immunoglobulin heavy constant epsilon (P01854) · a predicted model of the same protein · chain A against A, TM-score 0.92

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