Research workbench
AlphaFold monomer V2.0 prediction for DNA replication terminus site- binding protein (B5RAJ1)
Analyse AlphaFold monomer V2.0 prediction for DNA replication terminus site- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5RAJ1
- Type
- protein
- Length
- 309 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x507b0cF5c2F663afF8A05761eBf4e0Bf457a72Fb
- Molecule
- DNA replication terminus site-binding protein
- UniProt
- B5RAJ1
- Pockets
- 3 · best druggability 0.62
Structure
1 distinct chain · 38% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DNA replication terminus site-binding protein | protein | 309 | 38% helix, 27% strand | B5RAJ1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 355 | 0.62 | 0.78 | 43 | empty |
| 2 | 103 | 0.37 | 0.74 | 22 | empty |
| 3 | 105 | 0.35 | 0.74 | 15 | 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 B5RAJ1
- Elsewhere: UniProt B5RAJ1 · AlphaFold DB B5RAJ1
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