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Literature summary for 1.16.1.8 extracted from
- ELDOR spectroscopy reveals that energy landscapes in human methionine synthase reductase are extensively remodelled following ligand and partner protein binding (2011), ChemBioChem, 12, 863-867.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | the inferred multidomain structure of MSR and the presence of a large linker between the component flavin-containing domains suggest a large degree of conformational flexibility in the protein. MSR fluctuates between closed and open conformations, modeling, overview. Analysis of the complex structure formed between MSR, NADP+ and MS activation domain using the crystal structure, PDB ID 2QTZ, 2O2K, and 3ES9, overview | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Methionine synthase reductase | - |
Homo sapiens |
| MSR | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | - |
Homo sapiens |  |
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Release 2023.1 (January 2023)
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