Research workbench
AlphaFold monomer V2.0 prediction for disulfide bond formation protein B (Q5PCR9)
Analyse AlphaFold monomer V2.0 prediction for disulfide bond formation protein B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5PCR9
- Type
- protein
- Length
- 176 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9e5E98E011361C5888c92e2CDb7652E02Bd5C7Ed
- Molecule
- Disulfide bond formation protein B
- UniProt
- Q5PCR9
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 65% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disulfide bond formation protein B | protein | 176 | 65% helix, 2% strand | Q5PCR9 |
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 | 247 | 0.77 | 0.90 | 29 | empty |
| 2 | 66 | 0.38 | 0.78 | 12 | empty |
| 3 | 95 | 0.36 | 0.74 | 16 | empty |
Modifications
Observed in the structure: 2 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 Q5PCR9
- Elsewhere: UniProt Q5PCR9 · AlphaFold DB Q5PCR9
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