Research workbench
AlphaFold monomer V2.0 prediction for protein-methionine-sulfoxide reductase catalytic subunit msrp (B2VGX7)
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
- B2VGX7
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7782F4817b37743d738e9aF842bf74bd50f2015E
- Molecule
- Protein-methionine-sulfoxide reductase catalytic subunit msrp
- UniProt
- B2VGX7
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 30% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-methionine-sulfoxide reductase catalytic subunit msrp | protein | 334 | 30% helix, 23% strand | B2VGX7 |
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 | 370 | 0.71 | 0.82 | 52 | empty |
| 2 | 298 | 0.61 | 0.79 | 37 | empty |
| 3 | 151 | 0.41 | 0.74 | 26 | 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 B2VGX7
- Elsewhere: UniProt B2VGX7 · AlphaFold DB B2VGX7
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