Research workbench
AlphaFold monomer V2.0 prediction for protein-methionine-sulfoxide reductase catalytic subunit msrp (B5REX5)
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
- B5REX5
- Type
- protein
- Length
- 334 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xf409EF240fe4522BF573bd985931382e112b245C
- Molecule
- Protein-methionine-sulfoxide reductase catalytic subunit msrp
- UniProt
- B5REX5
- Pockets
- 4 · best druggability 0.72
Structure
1 distinct chain · 28% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein-methionine-sulfoxide reductase catalytic subunit msrp | protein | 334 | 28% helix, 22% strand | B5REX5 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 303 | 0.72 | 0.85 | 41 | empty |
| 2 | 145 | 0.60 | 0.84 | 18 | empty |
| 3 | 207 | 0.51 | 0.76 | 33 | empty |
| 4 | 64 | 0.37 | 0.78 | 22 | 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 B5REX5
- Elsewhere: UniProt B5REX5 · AlphaFold DB B5REX5
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