CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.720 | NAD(P)-binding Rossmann-like Domain |
Domain Context
CATH Clusters
| Superfamily | NAD(P)-binding Rossmann-like Domain |
| Functional Family | D-3-phosphoglycerate dehydrogenase |
Enzyme Information
| 1.1.1.95 |
Phosphoglycerate dehydrogenase.
based on mapping to UniProt P0A9T0
3-phospho-D-glycerate + NAD(+) = 3-phosphonooxypyruvate + NADH.
-!- Catalyzes the first committed and rate-limiting step in the phosphoserine pathway of serine biosynthesis. -!- The reaction occurs predominantly in the direction of reduction. -!- The enzyme from the bacterium Escherichia coli also catalyzes the activity of EC 1.1.1.399.
|
| 1.1.1.399 |
2-oxoglutarate reductase.
based on mapping to UniProt P0A9T0
(R)-2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + NADH.
-!- The enzyme catalyzes a reversible reaction. -!- The enzyme from the bacterium Peptoniphilus asaccharolyticus is specific for (R)-2-hydroxyglutarate. -!- The SerA enzyme from Escherichia coli can also accept (S)-2- hydroxyglutarate with a much higher Km, and also catalyzes the activity of EC 1.1.1.95.
|
UniProtKB Entries (1)
| P0A9T0 |
SERA_ECOLI
Escherichia coli K-12
D-3-phosphoglycerate dehydrogenase
|
PDB Structure
| PDB | 1PSD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The allosteric ligand site in the Vmax-type cooperative enzyme phosphoglycerate dehydrogenase.
Nat.Struct.Biol.
|
