Research workbench
AlphaFold monomer V2.0 prediction for 5,10-methylenetetrahydrofolate reductase (P45208)
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
- P45208
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xDd175FDc2561f3a80D6d56bCDE090F8cA47DD5f0
- UniProt
- P45208
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 292 | — | P45208 |
Compared structures
- 5UME · Crystal structure of 5,10-methylenetetrahydrofolate reductase metf from haemophilus… · an experimental structure of the same protein · chain A against E, TM-score 0.98
- 5UME · Crystal Structure of 5,10-Methylenetetrahydrofolate Reductase MetF from Haemophilus… · an experimental structure of the same protein · chain A against E, 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 P45208
- Elsewhere: UniProt P45208 · AlphaFold DB P45208
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