Research workbench
AlphaFold monomer V2.0 prediction for protein-methionine-sulfoxide reductase heme-binding subunit msrq (A9MCR7)
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
- A9MCR7
- Type
- protein
- Length
- 220 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x21ec5109EE01C0d4D6bcB2E62cbe36fe671Fafd7
- Molecule
- Protein-methionine-sulfoxide reductase heme-binding subunit msrq
- UniProt
- A9MCR7
- Pockets
- 2 · best druggability 0.71
Structure
1 distinct chain · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-methionine-sulfoxide reductase heme-binding subunit msrq | protein | 220 | 72% helix, 0% strand | A9MCR7 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 203 | 0.71 | 0.87 | 30 | empty |
| 2 | 115 | 0.55 | 0.83 | 23 | 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 A9MCR7
- Elsewhere: UniProt A9MCR7 · AlphaFold DB A9MCR7
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