Research workbench
Human high affinity Fc receptor FC(EPSILON)RI(ALPHA), monoclinic crystal form 2
Analyse Human high affinity Fc receptor FC(EPSILON)RI(ALPHA), monoclinic crystal form 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1J86
- Type
- protein
- Length
- 347 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- High affinity immunoglobulin epsilon receptor alpha- subunit
- UniProt
- P12319
- Ligands
- NAG, BMA, MAN, FCA
- Pockets
- 5 · best druggability 0.45
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | High affinity immunoglobulin epsilon receptor alpha- subunit | protein | 174 | 7% helix, 45% strand | P12319 |
| B | High affinity immunoglobulin epsilon receptor alpha- subunit | protein | 173 | 5% helix, 50% strand | P12319 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 16 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- FCA · alpha-D-fucopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 125 | 0.45 | 0.77 | 20 | empty |
| 2 | 74 | 0.42 | 0.80 | 20 | empty |
| 3 | 73 | 0.40 | 0.79 | 18 | empty |
| 4 | 152 | 0.40 | 0.73 | 16 | empty |
| 5 | 101 | 0.35 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 289 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 glycan, 4 disulfide (N-glycosylation, disulfide).
Compared structures
- 1J86 · Human high affinity Fc receptor FC(EPSILON)RI(ALPHA), monoclinic crystal form 2 · 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 B against A, TM-score 0.97
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 1J86 · PDBe 1J86 · UniProt P12319
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