Research workbench
AlphaFold monomer V2.0 prediction for phd finger protein 11 (Q2HJ93)
Analyse AlphaFold monomer V2.0 prediction for phd finger protein 11 (Q2HJ93) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2HJ93
- Type
- protein
- Length
- 337 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Phd finger protein 11
- UniProt
- Q2HJ93
- Pockets
- 4 · best druggability 0.48
Structure
1 distinct chain · 39% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phd finger protein 11 | protein | 337 | 39% helix, 9% strand | Q2HJ93 |
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 | 184 | 0.48 | 0.76 | 29 | empty |
| 2 | 125 | 0.44 | 0.77 | 23 | empty |
| 3 | 119 | 0.41 | 0.76 | 15 | empty |
| 4 | 79 | 0.34 | 0.75 | 24 | 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 Q2HJ93
- Elsewhere: UniProt Q2HJ93 · AlphaFold DB Q2HJ93
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