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AlphaFold monomer V2.0 prediction for BTB/POZ domain and ankyrin repeat-containing protein NPR5 (A2CIR7)
Analyse AlphaFold monomer V2.0 prediction for BTB/POZ domain and ankyrin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2CIR7
- Type
- protein
- Length
- 506 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0EA189b2343A464f560b44103f6A3396Da1dA8a9
- Molecule
- BTB/POZ domain and ankyrin repeat-containing protein NPR5
- UniProt
- A2CIR7
- Pockets
- 4 · best druggability 0.41
Structure
1 distinct chain · 49% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BTB/POZ domain and ankyrin repeat-containing protein NPR5 | protein | 506 | 49% helix, 3% strand | A2CIR7 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 127 | 0.41 | 0.75 | 20 | empty |
| 2 | 81 | 0.38 | 0.76 | 14 | empty |
| 3 | 62 | 0.32 | 0.76 | 15 | empty |
| 4 | 54 | 0.26 | 0.73 | 13 | 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 A2CIR7
- Elsewhere: UniProt A2CIR7 · AlphaFold DB A2CIR7
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