Research workbench
AlphaFold monomer V2.0 prediction for riboflavin biosynthesis protein ribba (Q5HNE3)
Analyse AlphaFold monomer V2.0 prediction for riboflavin biosynthesis protein ribba… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5HNE3
- Type
- protein
- Length
- 393 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9DF183349B8fe79e50431aA1CD89D989926F9f0f
- Molecule
- Riboflavin biosynthesis protein ribba
- UniProt
- Q5HNE3
- Pockets
- 4 · best druggability 0.78
Structure
1 distinct chain · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Riboflavin biosynthesis protein ribba | protein | 393 | 36% helix, 24% strand | Q5HNE3 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 242 | 0.78 | 0.91 | 39 | empty |
| 2 | 213 | 0.48 | 0.75 | 31 | empty |
| 3 | 65 | 0.40 | 0.80 | 17 | empty |
| 4 | 66 | 0.35 | 0.76 | 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 Q5HNE3
- Elsewhere: UniProt Q5HNE3 · AlphaFold DB Q5HNE3
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