Research workbench
AlphaFold monomer V2.0 prediction for replication protein a 70 kda DNA-binding subunit (Q5FW17)
Analyse AlphaFold monomer V2.0 prediction for replication protein a 70 kda DNA-binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5FW17
- Type
- protein
- Length
- 609 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8D2e4Aa2bf04A7561b24Ce08Ad813be6bD22A2B0
- Molecule
- Replication protein a 70 kda DNA-binding subunit
- UniProt
- Q5FW17
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 17% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Replication protein a 70 kda DNA-binding subunit | protein | 609 | 17% helix, 38% strand | Q5FW17 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 995 | 0.71 | 0.75 | 71 | empty |
| 2 | 340 | 0.56 | 0.75 | 46 | empty |
| 3 | 177 | 0.48 | 0.76 | 34 | empty |
| 4 | 102 | 0.45 | 0.79 | 24 | 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 Q5FW17
- Elsewhere: UniProt Q5FW17 · AlphaFold DB Q5FW17
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