Research workbench
AlphaFold monomer V2.0 prediction for 5,10-methylenetetrahydrofolate reductase (Q9JZQ3)
Analyse AlphaFold monomer V2.0 prediction for 5,10-methylenetetrahydrofolate reductase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9JZQ3
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
- UniProt
- Q9JZQ3
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 292 | — | Q9JZQ3 |
Compared structures
- 7RML · Neisseria meningitidis Methylenetetrahydrofolate reductase in complex with FAD · an experimental structure of the same protein · chain A against A, TM-score 0.95
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 Q9JZQ3
- Elsewhere: UniProt Q9JZQ3 · AlphaFold DB Q9JZQ3
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