Research workbench
AlphaFold monomer V2.0 prediction for UPF0761 membrane protein RRU_A2625 (Q2RR23)
Analyse AlphaFold monomer V2.0 prediction for UPF0761 membrane protein RRU_A2625… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2RR23
- Type
- protein
- Length
- 440 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC3Bd79E88714EbaDaCeF9C2A7Aa4f6E58AFE8289
- Molecule
- UPF0761 membrane protein RRU_A2625
- UniProt
- Q2RR23
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 74% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | UPF0761 membrane protein RRU_A2625 | protein | 440 | 74% helix, 2% strand | Q2RR23 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1139 | 0.71 | 0.74 | 80 | empty |
| 2 | 51 | 0.34 | 0.79 | 12 | empty |
| 3 | 53 | 0.26 | 0.72 | 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 Q2RR23
- Elsewhere: UniProt Q2RR23 · AlphaFold DB Q2RR23
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