Research workbench
AlphaFold monomer V2.0 prediction for replication factor C large subunit (A5UMF4)
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
- A5UMF4
- Type
- protein
- Length
- 492 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x2A70886e2AB13F20e22Df99DEc0896F1AC056Af4
- Molecule
- Replication factor C large subunit
- UniProt
- A5UMF4
- Pockets
- 2 · best druggability 0.62
Structure
1 distinct chain · 55% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Replication factor C large subunit | protein | 492 | 55% helix, 6% strand | A5UMF4 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.62 | 0.86 | 26 | empty |
| 2 | 78 | 0.39 | 0.78 | 20 | 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 A5UMF4
- Elsewhere: UniProt A5UMF4 · AlphaFold DB A5UMF4
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