MolNFT v1 · #172734 · protein
Structure of the S1-cleaved mouse NOTCH1 negative regulatory region (nrr)
7ABV · Neurogenic locus notch homolog protein 1: “Structure of the S1-cleaved mouse NOTCH1 negative regulatory region (nrr)”. X-ray diffraction, 2 ligands (NAG, CA), 3 pockets (best druggability 0.33). MolNFT v1 #172734 on GenesisL1: 3D…
- PDB
- 7ABV
- Type
- protein
- Length
- 232 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neurogenic locus notch homolog protein 1
- UniProt
- Q01705
- Ligands
- NAG, CA
- Pockets
- 3 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Neurogenic locus notch homolog protein 1 | protein | 232 | 38% helix, 15% strand | Q01705 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- CA · Calcium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 74 | 0.33 | 0.75 | 17 | empty |
| 2 | 59 | 0.33 | 0.76 | 15 | empty |
| 3 | 84 | 0.31 | 0.73 | 19 | empty |
Modifications
Observed in the structure: 10 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 7ABV · Structure of the S1-cleaved mouse Notch1 Negative Regulatory Region (NRR) · 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 0.98
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 7ABV · PDBe 7ABV · UniProt Q01705
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