Research workbench
AlphaFold monomer V2.0 prediction for DNA ligase (O33102)
Analyse AlphaFold monomer V2.0 prediction for DNA ligase (O33102) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O33102
- Type
- protein
- Length
- 694 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x29F5a997C9c963C0f8d9eA83ae506aA675743654
- Molecule
- DNA ligase
- UniProt
- O33102
- Pockets
- 8 · best druggability 0.79
Structure
1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA ligase | protein | 694 | 38% helix, 21% strand | O33102 |
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 809 | 0.79 | 0.82 | 78 | empty |
| 2 | 252 | 0.57 | 0.78 | 30 | empty |
| 3 | 156 | 0.52 | 0.80 | 23 | empty |
| 4 | 213 | 0.48 | 0.75 | 31 | empty |
| 5 | 134 | 0.42 | 0.76 | 18 | 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 O33102
- Elsewhere: UniProt O33102 · AlphaFold DB O33102
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