MolNFT v1 · #10958 · protein
Human high affinity Fc receptor FC(EPSILON)RI(ALPHA), hexagonal crystal form 1
1J87 · High affinity immunoglobulin epsilon receptor alpha- subunit: “Human high affinity Fc receptor FC(EPSILON)RI(ALPHA), hexagonal crystal form 1”. X-ray diffraction, 4 ligands (NAG, MAN, BMA), 2 pockets (best druggability 0.36). MolNFT…
- PDB
- 1J87
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High affinity immunoglobulin epsilon receptor alpha- subunit
- UniProt
- P12319
- Ligands
- NAG, MAN, BMA, FUC
- Pockets
- 2 · best druggability 0.36
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High affinity immunoglobulin epsilon receptor alpha- subunit | protein | 168 | 4% helix, 52% strand | P12319 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A
- BMA · beta-D-mannopyranose · sugar · chains A
- FUC · alpha-L-fucopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 114 | 0.36 | 0.73 | 16 | empty |
| 2 | 68 | 0.33 | 0.76 | 14 | empty |
Modifications
Observed in the structure: 4 glycan, 2 disulfide (N-glycosylation, disulfide).
Compared structures
- 1J87 · Human high affinity Fc receptor FC(EPSILON)RI(ALPHA), hexagonal crystal form 1 · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.94
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
- Elsewhere: RCSB PDB 1J87 · PDBe 1J87 · UniProt P12319
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