Research workbench
AlphaFold monomer V2.0 prediction for major MR/P fimbria protein (Q03011)
Analyse AlphaFold monomer V2.0 prediction for major MR/P fimbria protein (Q03011) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q03011
- Type
- protein
- Length
- 175 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- Major MR/P fimbria protein
- UniProt
- Q03011
- Pockets
- 1 · best druggability 0.58
Structure
1 distinct chain · 6% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major MR/P fimbria protein | protein | 175 | 6% helix, 35% strand | Q03011 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 189 | 0.58 | 0.80 | 23 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q03011
- Elsewhere: UniProt Q03011 · AlphaFold DB Q03011
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