Research workbench
Structure of the human IgE-Fc bound to its high affinity receptor FC(EPSILON)RI(ALPHA)
Analyse Structure of the human IgE-Fc bound to its high affinity receptor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F6A
- Type
- protein
- Length
- 606 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P12319, P01854
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 173 | — | P12319 |
| B | — | protein | 217 | — | P01854 |
| D | — | protein | 216 | — | P01854 |
Compared structures
- 1F6A · Structure of the human ige-fc bound to its high affinity receptor fc(epsilon)ri(alpha) · 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 D against A, TM-score 0.94
- P12319 · AlphaFold monomer V2.0 prediction for high affinity immunoglobulin epsilon receptor… · a predicted model of the same protein · chain A against A, TM-score 0.93
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P12319
- Every structure of UniProt P01854
- Elsewhere: RCSB PDB 1F6A · PDBe 1F6A · UniProt P12319 · UniProt P01854
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