Research workbench
AlphaFold monomer V2.0 prediction for replication factor C large subunit (A3DNV8)
Analyse AlphaFold monomer V2.0 prediction for replication factor C large subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3DNV8
- Type
- protein
- Length
- 423 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x8a5B95E954a528c22D7B40E74f98EdDe93dDf258
- Molecule
- Replication factor C large subunit
- UniProt
- A3DNV8
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 63% helix, 8% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Replication factor C large subunit | protein | 423 | 63% helix, 8% strand | A3DNV8 |
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 | 180 | 0.69 | 0.87 | 32 | empty |
| 2 | 54 | 0.36 | 0.79 | 10 | empty |
| 3 | 70 | 0.29 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 A3DNV8
- Elsewhere: UniProt A3DNV8 · AlphaFold DB A3DNV8
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