CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.10 | Roll | |
3.10.20 | Ubiquitin-like (UB roll) | |
3.10.20.70 | Glutamine synthetase, N-terminal domain |
Domain Context
CATH Clusters
Superfamily | Glutamine synthetase, N-terminal domain |
Functional Family | Glutamine synthetase |
Enzyme Information
2.3.1.225 |
Protein S-acyltransferase.
based on mapping to UniProt P15104
Palmitoyl-CoA + [protein]-L-cysteine = [protein]-S-palmitoyl-L-cysteine + CoA.
-!- The enzyme catalyzes the posttranslational protein palmitoylation that plays a role in protein-membrane interactions, protein trafficking, and enzyme activity. -!- Palmitoylation increases the hydrophobicity of proteins or protein domains and contributes to their membrane association.
|
6.3.1.2 |
Glutamine synthetase.
based on mapping to UniProt P15104
ATP + L-glutamate + NH(3) = ADP + phosphate + L-glutamine.
-!- Glutamine synthetase, which catalyzes the incorporation of ammonium into glutamate, is a key enzyme of nitrogen metabolism found in all domains of life. -!- Several types have been described, differing in their oligomeric structures and cofactor requirements.
|
UniProtKB Entries (1)
P15104 |
GLNA_HUMAN
Homo sapiens
Glutamine synthetase
|
PDB Structure
PDB | 2OJW |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal structures of mammalian glutamine synthetases illustrate substrate-induced conformational changes and provide opportunities for drug and herbicide design.
J.Mol.Biol.
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