Research workbench
AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (Q2NEA8)
Analyse AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (Q2NEA8) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q2NEA8
- Type
- protein
- Length
- 422 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x79a905d858Ce72991FD6E7a9C6498620f42E146D
- Molecule
- Serine hydroxymethyltransferase
- UniProt
- Q2NEA8
- Pockets
- 2 · best druggability 0.58
Structure
1 distinct chain · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine hydroxymethyltransferase | protein | 422 | 46% helix, 13% strand | Q2NEA8 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 317 | 0.58 | 0.76 | 26 | empty |
| 2 | 93 | 0.36 | 0.75 | 18 | 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 Q2NEA8
- Elsewhere: UniProt Q2NEA8 · AlphaFold DB Q2NEA8
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