Research workbench
AlphaFold monomer V2.0 prediction for pr domain zinc finger protein 15 (P57071)
Analyse AlphaFold monomer V2.0 prediction for pr domain zinc finger protein 15 (P57071) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P57071
- Type
- protein
- Length
- 1,507 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xCe4913b38f6cdd39cE5A2503280B7fe0683920B8
- Molecule
- Pr domain zinc finger protein 15
- UniProt
- P57071
- Pockets
- 6 · best druggability 0.60
Structure
1 distinct chain · 15% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pr domain zinc finger protein 15 | protein | 1507 | 15% helix, 8% strand | P57071 |
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 | 387 | 0.60 | 0.76 | 39 | empty |
| 2 | 257 | 0.56 | 0.77 | 34 | empty |
| 3 | 280 | 0.55 | 0.76 | 29 | empty |
| 4 | 159 | 0.50 | 0.77 | 20 | empty |
| 5 | 195 | 0.47 | 0.74 | 22 | empty |
Modifications
Observed in the structure: 3 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 P57071
- Elsewhere: UniProt P57071 · AlphaFold DB P57071
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