Research workbench
AlphaFold monomer V2.0 prediction for replication protein a 70 kda DNA-binding subunit B (Q10Q08)
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
- Q10Q08
- Type
- protein
- Length
- 630 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x639870EDE39Ab857257B9Fd8C31ebe8E02b985Ac
- Molecule
- Replication protein a 70 kda DNA-binding subunit B
- UniProt
- Q10Q08
- Pockets
- 6 · best druggability 0.52
Structure
1 distinct chain · 18% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Replication protein a 70 kda DNA-binding subunit B | protein | 630 | 18% helix, 36% strand | Q10Q08 |
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 | 312 | 0.52 | 0.74 | 42 | empty |
| 2 | 201 | 0.44 | 0.73 | 36 | empty |
| 3 | 140 | 0.41 | 0.74 | 19 | empty |
| 4 | 108 | 0.37 | 0.74 | 19 | empty |
| 5 | 53 | 0.28 | 0.75 | 12 | 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 Q10Q08
- Elsewhere: UniProt Q10Q08 · AlphaFold DB Q10Q08
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