Research workbench
AlphaFold monomer V2.0 prediction for DNA ligase (Q5V4R0)
Analyse AlphaFold monomer V2.0 prediction for DNA ligase (Q5V4R0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5V4R0
- Type
- protein
- Length
- 554 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x05D249E48b5e19C17E7AE90Ad57354470160c428
- Molecule
- DNA ligase
- UniProt
- Q5V4R0
- Pockets
- 6 · best druggability 0.63
Structure
1 distinct chain · 43% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA ligase | protein | 554 | 43% helix, 22% strand | Q5V4R0 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 242 | 0.63 | 0.81 | 27 | empty |
| 2 | 192 | 0.42 | 0.73 | 23 | empty |
| 3 | 60 | 0.40 | 0.81 | 13 | empty |
| 4 | 114 | 0.39 | 0.75 | 24 | empty |
| 5 | 109 | 0.34 | 0.73 | 20 | 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 Q5V4R0
- Elsewhere: UniProt Q5V4R0 · AlphaFold DB Q5V4R0
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