CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.990 | NADPH-cytochrome p450 Reductase; Chain A, domain 3 |
|
1.20.990.10 | NADPH-cytochrome p450 Reductase; Chain A, domain 3 |
Domain Context
CATH Clusters
| Superfamily | NADPH-cytochrome p450 Reductase; Chain A, domain 3 |
| Functional Family | Methionine synthase reductase |
Enzyme Information
| 1.16.1.8 |
[Methionine synthase] reductase.
based on mapping to UniProt Q9UBK8
2 [methionine synthase]-methylcob(III)alamin + 2 S-adenosylhomocysteine + NADP(+) = 2 [methionine synthase]-cob(II)alamin + NADPH + 2 S-adenosyl-L- methionine.
-!- The substrate of the enzyme is the inactivated cobalt(II) form of EC 2.1.1.13. -!- Electrons are transferred from NADPH to FAD to FMN. -!- Formerly EC 2.1.1.135.
|
UniProtKB Entries (1)
| Q9UBK8 |
MTRR_HUMAN
Homo sapiens
Methionine synthase reductase
|
PDB Structure
| PDB | 2QTL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Mechanism of Coenzyme Binding to Human Methionine Synthase Reductase Revealed through the Crystal Structure of the FNR-like Module and Isothermal Titration Calorimetry
Biochemistry
|