Research workbench
AlphaFold monomer V2.0 prediction for DNA nucleotidylexotransferase (P36195)
Analyse AlphaFold monomer V2.0 prediction for DNA nucleotidylexotransferase (P36195) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P36195
- Type
- protein
- Length
- 506 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xEfeF22Cb92c4cdFf0004010904498915700e52C5
- Molecule
- DNA nucleotidylexotransferase
- UniProt
- P36195
- Pockets
- 5 · best druggability 0.69
Structure
1 distinct chain · 39% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA nucleotidylexotransferase | protein | 506 | 39% helix, 13% strand | P36195 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 908 | 0.69 | 0.74 | 66 | empty |
| 2 | 51 | 0.62 | 0.92 | 15 | empty |
| 3 | 170 | 0.56 | 0.81 | 30 | empty |
| 4 | 173 | 0.44 | 0.74 | 30 | empty |
| 5 | 73 | 0.41 | 0.79 | 21 | 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 P36195
- Elsewhere: UniProt P36195 · AlphaFold DB P36195
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