Research workbench
AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (A1SUU0)
Analyse AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (A1SUU0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A1SUU0
- Type
- protein
- Length
- 421 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xB0E05376C9C95241a0229bD9FE1e93d0AacB321F
- UniProt
- A1SUU0
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 421 | — | A1SUU0 |
Compared structures
- 4P3M · Crystal structure of serine hydroxymethyltransferase from Psychromonas ingrahamii · an experimental structure of the same protein · chain A against B, TM-score 0.90
- 4P3M · Crystal structure of serine hydroxymethyltransferase from psychromonas ingrahamii · an experimental structure of the same protein · chain A against B, TM-score 0.90
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 A1SUU0
- Elsewhere: UniProt A1SUU0 · AlphaFold DB A1SUU0
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