MolNFT v1 · #540853 · protein
AlphaFold monomer V2.0 prediction for zinc finger mynd domain- containing protein 10 (O75800)
O75800 · Zinc finger mynd domain-containing protein 10: “AlphaFold monomer V2.0 prediction for zinc finger mynd domain- containing protein 10 (O75800)”. 8 pockets (best druggability 0.70). MolNFT v1 #540853 on GenesisL1: 3D structure…
- Accession
- O75800
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4d07E6a23DeB6B95bd9b90EcB67368b7e8D3B77e
- Molecule
- Zinc finger mynd domain-containing protein 10
- UniProt
- O75800
- Pockets
- 8 · best druggability 0.70
Structure
1 distinct chain · 64% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Zinc finger mynd domain-containing protein 10 | protein | 440 | 64% helix, 5% strand | O75800 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 764 | 0.70 | 0.77 | 53 | empty |
| 2 | 177 | 0.51 | 0.78 | 18 | empty |
| 3 | 216 | 0.48 | 0.74 | 23 | empty |
| 4 | 111 | 0.41 | 0.76 | 16 | empty |
| 5 | 104 | 0.37 | 0.74 | 18 | empty |
Compared structures
- 2D8Q · Solution structure of the MYND domain of the human zinc finger MYND domain-containing… · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 2D8Q · Solution structure of the mynd domain of the human zinc finger mynd domain-containing… · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 2DAN · The solution structure of the MYND domain (LEU384-CYS430) of human Zinc finger MYND… · an experimental structure of the same protein · chain A against A, TM-score 0.12
- 2DAN · The solution structure of the mynd domain (LEU384-CYS430) of human zinc finger mynd… · an experimental structure of the same protein · chain A against A, TM-score 0.12
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 O75800
- Elsewhere: UniProt O75800 · AlphaFold DB O75800
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