Research workbench
AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (P0A825)
Analyse AlphaFold monomer V2.0 prediction for serine hydroxymethyltransferase (P0A825) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P0A825
- Type
- protein
- Length
- 417 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x67446C1700CC93ef0254b222f4f1f1f77F376633
- UniProt
- P0A825
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 417 | — | P0A825 |
Compared structures
- 1DFO · Crystal structure at 2.4 ångström resolution of E. COLI serine hydroxymethyltransferase… · an experimental structure of the same protein · chain A against B, TM-score 1.00
- 1DFO · Crystal structure at 2.4 ångström resolution of E. COLI serine hydroxymethyltransferase… · an experimental structure of the same protein · chain A against B, TM-score 1.00
- 3G8M · Serine hydroxymethyltransferase Y55F mutant · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 3G8M · Serine Hydroxymethyltransferase Y55F Mutant · an experimental structure of the same protein · chain A against A, TM-score 0.98
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 P0A825
- Elsewhere: UniProt P0A825 · AlphaFold DB P0A825
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