Research workbench
AlphaFold monomer V2.0 prediction for flagellar L-ring protein (C0RKA1)
Analyse AlphaFold monomer V2.0 prediction for flagellar L-ring protein (C0RKA1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C0RKA1
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- Flagellar L-ring protein
- UniProt
- C0RKA1
- Pockets
- 2 · best druggability 0.32
Structure
1 distinct chain · 19% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flagellar L-ring protein | protein | 238 | 19% helix, 40% strand | C0RKA1 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 89 | 0.32 | 0.73 | 17 | empty |
| 2 | 55 | 0.27 | 0.74 | 18 | 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 C0RKA1
- Elsewhere: UniProt C0RKA1 · AlphaFold DB C0RKA1
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