Research workbench
AlphaFold monomer V2.0 prediction for protein qua-1 (G5EC21)
Analyse AlphaFold monomer V2.0 prediction for protein qua-1 (G5EC21) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- G5EC21
- Type
- protein
- Length
- 1,169 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x07c85d409125bF6733584D6f9a3330A838724e87
- Molecule
- Protein qua-1
- UniProt
- G5EC21
- Pockets
- 6 · best druggability 0.74
Structure
1 distinct chain · 7% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein qua-1 | protein | 1169 | 7% helix, 15% strand | G5EC21 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 999 | 0.74 | 0.77 | 95 | empty |
| 2 | 261 | 0.56 | 0.77 | 37 | empty |
| 3 | 242 | 0.52 | 0.76 | 44 | empty |
| 4 | 96 | 0.45 | 0.80 | 24 | empty |
| 5 | 51 | 0.30 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 6 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 G5EC21
- Elsewhere: UniProt G5EC21 · AlphaFold DB G5EC21
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