Research workbench
Crystal structure of juno, the mammalian egg receptor for sperm IZUMO1
Analyse Crystal structure of juno, the mammalian egg receptor for sperm IZUMO1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EJN
- Type
- protein
- Length
- 338 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sperm-egg fusion protein juno
- UniProt
- Q9EQF4
- Ligands
- NAG
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sperm-egg fusion protein juno | protein | 166 | 40% helix, 9% strand | Q9EQF4 |
| B | Sperm-egg fusion protein juno | protein | 172 | 40% helix, 10% strand | Q9EQF4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 476 | 0.70 | 0.80 | 40 | empty |
| 2 | 221 | 0.55 | 0.78 | 31 | empty |
| 3 | 177 | 0.50 | 0.77 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 158 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 5EJN · Crystal structure of Juno, the mammalian egg receptor for sperm Izumo1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9EQF4 · AlphaFold monomer V2.0 prediction for sperm-egg fusion protein juno (Q9EQF4) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 Q9EQF4
- Elsewhere: RCSB PDB 5EJN · PDBe 5EJN · UniProt Q9EQF4
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