Research workbench
AlphaFold monomer V2.0 prediction for endoplasmic reticulum membrane sensor NFE2L1 (Q5ZL67)
Analyse AlphaFold monomer V2.0 prediction for endoplasmic reticulum membrane sensor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5ZL67
- Type
- protein
- Length
- 772 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x362a6d063b1B7E1B6EfD3A9A7CA3612e3FE037AA
- Molecule
- Endoplasmic reticulum membrane sensor NFE2L1
- UniProt
- Q5ZL67
- Pockets
- 3 · best druggability 0.47
Structure
1 distinct chain · 33% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoplasmic reticulum membrane sensor NFE2L1 | protein | 772 | 33% helix, 3% strand | Q5ZL67 |
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 | 137 | 0.47 | 0.78 | 17 | empty |
| 2 | 211 | 0.46 | 0.73 | 25 | empty |
| 3 | 129 | 0.42 | 0.76 | 20 | empty |
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 Q5ZL67
- Elsewhere: UniProt Q5ZL67 · AlphaFold DB Q5ZL67
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