Research workbench
AlphaFold monomer V2.0 prediction for ribonuclease E/G-like protein (P51211)
Analyse AlphaFold monomer V2.0 prediction for ribonuclease E/G-like protein (P51211) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P51211
- Type
- protein
- Length
- 511 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x493A46D594a1E8e8D0cF404bE2e0aEf46432960F
- Molecule
- Ribonuclease E/G-like protein
- UniProt
- P51211
- Pockets
- 7 · best druggability 0.74
Structure
1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ribonuclease E/G-like protein | protein | 511 | 33% helix, 22% strand | P51211 |
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 944 | 0.74 | 0.78 | 74 | empty |
| 2 | 433 | 0.63 | 0.76 | 36 | empty |
| 3 | 271 | 0.57 | 0.78 | 37 | empty |
| 4 | 258 | 0.55 | 0.76 | 35 | empty |
| 5 | 79 | 0.41 | 0.79 | 16 | 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 P51211
- Elsewhere: UniProt P51211 · AlphaFold DB P51211
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