CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.70 | Aldolase class I |
Domain Context
CATH Clusters
| Superfamily | Aldolase class I |
| Functional Family | Fructose-bisphosphate aldolase |
Enzyme Information
| 4.1.2.13 |
Fructose-bisphosphate aldolase.
based on mapping to UniProt P00883
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.
-!- Also acts on (3S,4R)-ketose 1-phosphates. -!- The enzymes increase electron-attraction by the carbonyl group, some (Class I) forming a protonated imine with it, others (Class II), mainly of microbial origin, polarizing it with a metal ion, e.g. zinc. -!- Formerly EC 4.1.2.7.
|
UniProtKB Entries (2)
| P00883 |
ALDOA_RABIT
Oryctolagus cuniculus
Fructose-bisphosphate aldolase A
|
| P42768 |
WASP_HUMAN
Homo sapiens
Wiskott-Aldrich syndrome protein
|
PDB Structure
| PDB | 2OT0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
A hydrophobic pocket in the active site of glycolytic aldolase mediates interactions with wiskott-Aldrich syndrome protein.
J.Biol.Chem.
|
