Research workbench
AlphaFold monomer V2.0 prediction for zinc metalloprotease RIP1 (Q9CBU4)
Analyse AlphaFold monomer V2.0 prediction for zinc metalloprotease RIP1 (Q9CBU4) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9CBU4
- Type
- protein
- Length
- 404 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Zinc metalloprotease RIP1
- UniProt
- Q9CBU4
- Pockets
- 3 · best druggability 0.74
Structure
1 distinct chain · 48% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc metalloprotease RIP1 | protein | 404 | 48% helix, 22% strand | Q9CBU4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1135 | 0.74 | 0.77 | 81 | empty |
| 2 | 152 | 0.50 | 0.78 | 23 | empty |
| 3 | 64 | 0.30 | 0.74 | 11 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q9CBU4
- Elsewhere: UniProt Q9CBU4 · AlphaFold DB Q9CBU4
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