Research workbench
AlphaFold monomer V2.0 prediction for replication factor C subunit 3 (Q8R323)
Analyse AlphaFold monomer V2.0 prediction for replication factor C subunit 3 (Q8R323) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8R323
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xc0F878C3f3E2a1874e2A6daC80d429e553DdB0D5
- Molecule
- Replication factor C subunit 3
- UniProt
- Q8R323
- Pockets
- 5 · best druggability 0.67
Structure
1 distinct chain · 59% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Replication factor C subunit 3 | protein | 356 | 59% helix, 12% strand | Q8R323 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 202 | 0.67 | 0.85 | 32 | empty |
| 2 | 138 | 0.39 | 0.74 | 23 | empty |
| 3 | 81 | 0.37 | 0.77 | 20 | empty |
| 4 | 71 | 0.34 | 0.76 | 15 | empty |
| 5 | 73 | 0.28 | 0.72 | 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 Q8R323
- Elsewhere: UniProt Q8R323 · AlphaFold DB Q8R323
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