Research workbench
Crystal structure of the human sperm IZUMO1 residues 22-268
Analyse Crystal structure of the human sperm IZUMO1 residues 22-268 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5F4V
- Type
- protein
- Length
- 235 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Izumo sperm-egg fusion protein 1
- UniProt
- Q8IYV9
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Izumo sperm-egg fusion protein 1 | protein | 235 | 42% helix, 31% strand | Q8IYV9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 5F4V · Crystal structure of the human sperm Izumo1 residues 22-268 · the same entry in another collection · chain A against A, TM-score 1.00
- Q8IYV9 · AlphaFold monomer V2.0 prediction for izumo sperm-egg fusion protein 1 (Q8IYV9) · a predicted model of the same protein · chain A against A, TM-score 0.83
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 Q8IYV9
- Elsewhere: RCSB PDB 5F4V · PDBe 5F4V · UniProt Q8IYV9
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