Research workbench
AlphaFold monomer V2.0 prediction for protein NLRC5 (C6FG12)
Analyse AlphaFold monomer V2.0 prediction for protein NLRC5 (C6FG12) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C6FG12
- Type
- protein
- Length
- 1,726 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBF0D2e107Ce1EcD2C4369B042274201DB719AaAF
- Molecule
- Protein NLRC5
- UniProt
- C6FG12
- Pockets
- 20 · best druggability 0.82
Structure
1 distinct chain · 42% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein NLRC5 | protein | 1726 | 42% helix, 17% strand | C6FG12 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 825 | 0.82 | 0.84 | 66 | empty |
| 2 | 654 | 0.81 | 0.85 | 54 | empty |
| 3 | 57 | 0.67 | 0.95 | 18 | empty |
| 4 | 50 | 0.66 | 0.95 | 16 | empty |
| 5 | 75 | 0.57 | 0.88 | 23 | 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 C6FG12
- Elsewhere: UniProt C6FG12 · AlphaFold DB C6FG12
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