Research workbench
AlphaFold monomer V2.0 prediction for bardet-biedl syndrome 4 protein homolog (Q5CZ52)
Analyse AlphaFold monomer V2.0 prediction for bardet-biedl syndrome 4 protein homolog… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5CZ52
- Type
- protein
- Length
- 462 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5Ded1C9cb4c4020CEee9D7f2723AAB1C7B706Fd9
- Molecule
- Bardet-biedl syndrome 4 protein homolog
- UniProt
- Q5CZ52
- Pockets
- 4 · best druggability 0.34
Structure
1 distinct chain · 66% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bardet-biedl syndrome 4 protein homolog | protein | 462 | 66% helix, 1% strand | Q5CZ52 |
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 | 106 | 0.34 | 0.73 | 20 | empty |
| 2 | 100 | 0.34 | 0.73 | 15 | empty |
| 3 | 78 | 0.34 | 0.75 | 15 | empty |
| 4 | 87 | 0.31 | 0.72 | 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 Q5CZ52
- Elsewhere: UniProt Q5CZ52 · AlphaFold DB Q5CZ52
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