Research workbench
AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (B9LQJ1)
Analyse AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (B9LQJ1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B9LQJ1
- Type
- protein
- Length
- 415 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Serine hydroxymethyltransferase
- UniProt
- B9LQJ1
- Pockets
- 3 · best druggability 0.53
Structure
1 distinct chain · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine hydroxymethyltransferase | protein | 415 | 48% helix, 15% strand | B9LQJ1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 256 | 0.53 | 0.76 | 24 | empty |
| 2 | 141 | 0.43 | 0.76 | 30 | empty |
| 3 | 50 | 0.29 | 0.76 | 14 | 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 B9LQJ1
- Elsewhere: UniProt B9LQJ1 · AlphaFold DB B9LQJ1
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