Research workbench
AlphaFold monomer V2.0 prediction for 3'-5' exoribonuclease yham (B7IK95)
Analyse AlphaFold monomer V2.0 prediction for 3'-5' exoribonuclease yham (B7IK95) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B7IK95
- Type
- protein
- Length
- 314 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- Molecule
- 3'-5' exoribonuclease yham
- UniProt
- B7IK95
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3'-5' exoribonuclease yham | protein | 314 | 46% helix, 20% strand | B7IK95 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 607 | 0.67 | 0.77 | 52 | empty |
| 2 | 234 | 0.54 | 0.77 | 23 | empty |
| 3 | 57 | 0.29 | 0.74 | 13 | 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 B7IK95
- Elsewhere: UniProt B7IK95 · AlphaFold DB B7IK95
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