Research workbench
AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (A2REH5)
Analyse AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (A2REH5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2REH5
- Type
- protein
- Length
- 418 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb21ec8561536D7DEd13EC0Ed01b162cd7EB5dE01
- Molecule
- Serine hydroxymethyltransferase
- UniProt
- A2REH5
- Pockets
- 3 · best druggability 0.48
Structure
1 distinct chain · 47% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine hydroxymethyltransferase | protein | 418 | 47% helix, 14% strand | A2REH5 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 195 | 0.48 | 0.76 | 35 | empty |
| 2 | 185 | 0.45 | 0.74 | 21 | empty |
| 3 | 50 | 0.34 | 0.79 | 19 | 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 A2REH5
- Elsewhere: UniProt A2REH5 · AlphaFold DB A2REH5
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