UniProt Q5SLG6
Methylenetetrahydrofolate reductase (Q5SLG6)
Methylenetetrahydrofolate reductase (UniProt Q5SLG6), EC 1.5.1.20: 6 experimental structures on GenesisL1, 3 ligands bound, 16 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- Q5SLG6
- Protein
- Methylenetetrahydrofolate reductase
- EC
- 1.5.1.20
- Experimental structures
- 6
- Predicted models
- 0
- Ligands
- 3
- Pockets
- 16 · 2 records with a druggable one
Structures
6 records of Q5SLG6 in the MolNFT archive: 6 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 3APT | properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus… | x-ray diffraction | A, B | — | — |
| 3APT | Properties and crystal structure of methylenetetrahydrofolate reductase from thermus thermophilus… | x-ray diffraction | A, B | — | — |
| 3APY | Properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 3APY | Properties and crystal structure of methylenetetrahydrofolate reductase from thermus thermophilus… | x-ray diffraction | A, B, C, D, E, F, G, H | — | — |
| 7TH4 | T. thermophilus methylenetetrahydrofolate reductase complex with 5-formyltetrahydrofolate | x-ray diffraction | A, B | FAD, FFO, CL | 8 (best 0.76) |
| 8EAC | Thermus thermophilus methylenetetrahydrofolate reductase | x-ray diffraction | A, B | FAD | 8 (best 0.73) |
Ligands
Elsewhere
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