Research workbench
AlphaFold monomer V2.0 prediction for UV DNA damage endonuclease (B7HFP5)
Analyse AlphaFold monomer V2.0 prediction for UV DNA damage endonuclease (B7HFP5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7HFP5
- Type
- protein
- Length
- 317 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3BD960301fFCd02d42e55a21D409c3bD1BA31b78
- Molecule
- UV DNA damage endonuclease
- UniProt
- B7HFP5
- Pockets
- 2 · best druggability 0.49
Structure
1 distinct chain · 45% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UV DNA damage endonuclease | protein | 317 | 45% helix, 14% strand | B7HFP5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 240 | 0.49 | 0.74 | 36 | empty |
| 2 | 120 | 0.40 | 0.75 | 22 | 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 B7HFP5
- Elsewhere: UniProt B7HFP5 · AlphaFold DB B7HFP5
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