Research workbench
AlphaFold monomer V2.0 prediction for protein-methionine-sulfoxide reductase heme-binding subunit msrq (B5XNE5)
Analyse AlphaFold monomer V2.0 prediction for protein-methionine-sulfoxide reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5XNE5
- Type
- protein
- Length
- 199 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xaa53776A41fB2e67da75A96E8a53746b6874aAB4
- Molecule
- Protein-methionine-sulfoxide reductase heme-binding subunit msrq
- UniProt
- B5XNE5
- Pockets
- 3 · best druggability 0.77
Structure
1 distinct chain · 83% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-methionine-sulfoxide reductase heme-binding subunit msrq | protein | 199 | 83% helix, 0% strand | B5XNE5 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.77 | 0.91 | 36 | empty |
| 2 | 197 | 0.70 | 0.88 | 31 | empty |
| 3 | 51 | 0.28 | 0.74 | 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 B5XNE5
- Elsewhere: UniProt B5XNE5 · AlphaFold DB B5XNE5
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