Research workbench
AlphaFold monomer V2.0 prediction for DNA damage response protein kinase DUN1 (P39009)
Analyse AlphaFold monomer V2.0 prediction for DNA damage response protein kinase DUN1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P39009
- Type
- protein
- Length
- 513 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x576AbE9948fdf53cF041C558443887E553DF5B89
- Molecule
- DNA damage response protein kinase DUN1
- UniProt
- P39009
- Pockets
- 7 · best druggability 0.76
Structure
1 distinct chain · 22% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA damage response protein kinase DUN1 | protein | 513 | 22% helix, 25% strand | P39009 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 700 | 0.76 | 0.81 | 76 | empty |
| 2 | 116 | 0.40 | 0.75 | 19 | empty |
| 3 | 104 | 0.38 | 0.75 | 22 | empty |
| 4 | 98 | 0.38 | 0.75 | 18 | empty |
| 5 | 116 | 0.35 | 0.72 | 23 | empty |
Compared structures
- 2JQL · NMR structure of the yeast Dun1 FHA domain in complex with a doubly phosphorylated (pT)… · an experimental structure of the same protein · chain A against A, TM-score 0.23
- 2JQL · NMR structure of the yeast DUN1 fha domain in complex with a doubly phosphorylated (pt)… · an experimental structure of the same protein · chain A against A, TM-score 0.23
- 2JQJ · NMR structure of yeast Dun1 FHA domain · an experimental structure of the same protein · chain A against A, TM-score 0.21
- 2JQJ · NMR structure of yeast DUN1 fha domain · an experimental structure of the same protein · chain A against A, TM-score 0.21
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 P39009
- Elsewhere: UniProt P39009 · AlphaFold DB P39009
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