Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease E (A0R152)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease E (A0R152) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0R152
- Type
- protein
- Length
- 1,037 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaa53776A41fB2e67da75A96E8a53746b6874aAB4
- Molecule
- Ribonuclease E
- UniProt
- A0R152
- Pockets
- 7 · best druggability 0.75
Structure
1 distinct chain · 20% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease E | protein | 1037 | 20% helix, 13% strand | A0R152 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 826 | 0.75 | 0.79 | 97 | empty |
| 2 | 171 | 0.55 | 0.80 | 29 | empty |
| 3 | 154 | 0.53 | 0.80 | 20 | empty |
| 4 | 113 | 0.47 | 0.79 | 20 | empty |
| 5 | 176 | 0.47 | 0.75 | 22 | 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 A0R152
- Elsewhere: UniProt A0R152 · AlphaFold DB A0R152
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