Research workbench
AlphaFold monomer V2.0 prediction for DNA ligase (O87703)
Analyse AlphaFold monomer V2.0 prediction for DNA ligase (O87703) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O87703
- Type
- protein
- Length
- 670 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0D671490EE06E75975e90D7F99F73B20BE618744
- Molecule
- DNA ligase
- UniProt
- O87703
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA ligase | protein | 670 | 40% helix, 22% strand | O87703 |
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 | 742 | 0.76 | 0.81 | 73 | empty |
| 2 | 381 | 0.65 | 0.79 | 31 | empty |
| 3 | 133 | 0.52 | 0.81 | 26 | empty |
| 4 | 212 | 0.49 | 0.75 | 33 | empty |
| 5 | 116 | 0.36 | 0.73 | 17 | empty |
Compared structures
- 1B04 · Structure of the adenylation domain of an NAD+ dependent ligase · an experimental structure of the same protein · chain A against A, TM-score 0.46
- 1B04 · Structure of the adenylation domain of an NAD+ dependent ligase · an experimental structure of the same protein · chain A against A, TM-score 0.46
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 O87703
- Elsewhere: UniProt O87703 · AlphaFold DB O87703
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