Research workbench
AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (B5ELV3)
Analyse AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (B5ELV3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5ELV3
- Type
- protein
- Length
- 414 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3BB61284E47a075411d99C0E0F0AFdea58cF5CD6
- Molecule
- Serine hydroxymethyltransferase
- UniProt
- B5ELV3
- Pockets
- 2 · best druggability 0.45
Structure
1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine hydroxymethyltransferase | protein | 414 | 49% helix, 14% strand | B5ELV3 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 154 | 0.45 | 0.76 | 37 | empty |
| 2 | 143 | 0.42 | 0.75 | 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 B5ELV3
- Elsewhere: UniProt B5ELV3 · AlphaFold DB B5ELV3
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