Research workbench
AlphaFold monomer V2.0 prediction for large cysteine-rich periplasmic protein omcb, serovars I/J (Q933I7)
Analyse AlphaFold monomer V2.0 prediction for large cysteine-rich periplasmic protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q933I7
- Type
- protein
- Length
- 547 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- Molecule
- Large cysteine-rich periplasmic protein omcb, serovars I/J
- UniProt
- Q933I7
- Pockets
- 2 · best druggability 0.60
Structure
1 distinct chain · 7% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Large cysteine-rich periplasmic protein omcb, serovars I/J | protein | 547 | 7% helix, 54% strand | Q933I7 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 443 | 0.60 | 0.75 | 40 | empty |
| 2 | 90 | 0.40 | 0.77 | 22 | 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 Q933I7
- Elsewhere: UniProt Q933I7 · AlphaFold DB Q933I7
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