CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
 
	 | 
    3 | Alpha Beta | 
 
	 | 
    3.40 | 3-Layer(aba) Sandwich | 
 
	 | 
    3.40.630 | Aminopeptidase | 
 
	 | 
    3.40.630.170 | 
Domain Context
CATH Clusters
| Superfamily | 3.40.630.170 | 
| Functional Family | Glycylpeptide N-tetradecanoyltransferase | 
Enzyme Information
| 2.3.1.97 | 
							 Glycylpeptide N-tetradecanoyltransferase. 
							based on mapping to UniProt P30419 		
							Tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal- N-tetradecanoylglycyl-[protein]. 
							-!- The enzyme catalyzes the transfer of myristic acid from myristoyl-CoA to the amino group of the N-terminal glycine residue in a variety of eukaryotic proteins. -!- It uses an ordered Bi Bi reaction in which myristoyl-CoA binds to the enzyme prior to the binding of the peptide substrate, and CoA release precedes the release of the myristoylated peptide. -!- The enzyme from yeast is profoundly affected by amino acids further from the N-terminus, and is particularly stimulated by a serine residue at position 5. 
						 | 
					
UniProtKB Entries (1)
| P30419 | 
						 NMT1_HUMAN 
						Homo sapiens 
						Glycylpeptide N-tetradecanoyltransferase 1 
					 | 
				
PDB Structure
| PDB | 5MU6 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | 
					 Fragment-derived inhibitors of human N-myristoyltransferase block capsid assembly and replication of the common cold virus. 
					    
					    Nat Chem 
					    
					 | 
			
