Research workbench
AlphaFold monomer V2.0 prediction for disulfide bond formation protein B (Q63RY4)
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
- Q63RY4
- Type
- protein
- Length
- 169 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9073C46348542FfE4327c3F363F9B51B22058e75
- Molecule
- Disulfide bond formation protein B
- UniProt
- Q63RY4
- Pockets
- 1 · best druggability 0.71
Structure
1 distinct chain · 79% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disulfide bond formation protein B | protein | 169 | 79% helix, 1% strand | Q63RY4 |
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 | 168 | 0.71 | 0.89 | 27 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5VYO · The complex structure of burkholderia pseudomallei dsba bound to a peptide · an experimental structure of the same protein · chain A against H, TM-score 0.03
- 5VYO · The complex structure of Burkholderia pseudomallei DsbA bound to a peptide · an experimental structure of the same protein · chain A against H, TM-score 0.03
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 Q63RY4
- Elsewhere: UniProt Q63RY4 · AlphaFold DB Q63RY4
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