MolNFT v1 · #343691 · protein
AlphaFold monomer V2.0 prediction for telomere-associated protein RIF1 (E1C2U2)
E1C2U2: “AlphaFold monomer V2.0 prediction for telomere-associated protein RIF1 (E1C2U2)”. 10 pockets (best druggability 0.62). MolNFT v1 #343691 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- E1C2U2
- Type
- protein
- Length
- 2,326 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- Telomere-associated protein RIF1
- UniProt
- E1C2U2
- Pockets
- 10 · best druggability 0.62
Structure
1 distinct chain · 33% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Telomere-associated protein RIF1 | protein | 2326 | 33% helix, 0% strand | E1C2U2 |
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 580 | 0.62 | 0.74 | 54 | empty |
| 2 | 125 | 0.60 | 0.85 | 24 | empty |
| 3 | 199 | 0.44 | 0.73 | 24 | empty |
| 4 | 118 | 0.41 | 0.75 | 17 | empty |
| 5 | 108 | 0.39 | 0.75 | 17 | 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 E1C2U2
- Elsewhere: UniProt E1C2U2 · AlphaFold DB E1C2U2
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