Research workbench
AlphaFold monomer V2.0 prediction for bifunctional protein fold (Q5SJ94)
Analyse AlphaFold monomer V2.0 prediction for bifunctional protein fold (Q5SJ94) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5SJ94
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7c75F0f7d6d136A2b8D4C6C6e9b3D8a697949DF1
- UniProt
- Q5SJ94
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 282 | — | Q5SJ94 |
Compared structures
- 6V6Y · Crystal structure of T. thermophilus methylenetetrahydrofolate dehydrogenase (mthfd) · an experimental structure of the same protein · chain A against A, TM-score 0.97
- 6V6Y · Crystal Structure of T. thermophilus methylenetetrahydrofolate dehydrogenase (MTHFD) · an experimental structure of the same protein · chain A against A, TM-score 0.97
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 Q5SJ94
- Elsewhere: UniProt Q5SJ94 · AlphaFold DB Q5SJ94
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