Research workbench
Structure of O-fucosylated epidermal growth factor-like repeat 12 of mouse Notch-1 receptor
Analyse Structure of O-fucosylated epidermal growth factor-like repeat 12 of mouse… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RR2
- Type
- protein
- Length
- 38 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Molecule
- Neurogenic locus notch homolog protein 1
- UniProt
- Q01705
- Ligands
- FUC
Structure
solution nmr · resolution NOT · 1 distinct chain · 0% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neurogenic locus notch homolog protein 1 | protein | 38 | 0% helix, 11% strand | Q01705 |
Ligands and binding sites
- FUC · alpha-L-fucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide, 1 glycan (disulfide, O-glycosylation).
Compared structures
- 2RR2 · Structure of O-fucosylated epidermal growth factor-like repeat 12 of mouse notch-1… · the same entry in another collection · chain A against A, TM-score 1.00
- Q01705 · AlphaFold monomer V2.0 prediction for neurogenic locus notch homolog protein 1 (Q01705) · a predicted model of the same protein · chain A against A, TM-score 0.60
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 Q01705
- Elsewhere: RCSB PDB 2RR2 · PDBe 2RR2 · UniProt Q01705
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