CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
 
	 | 
    3 | Alpha Beta | 
 
	 | 
    3.40 | 3-Layer(aba) Sandwich | 
 
	 | 
    3.40.50 | Rossmann fold | 
 
	 | 
    3.40.50.1820 | alpha/beta hydrolase | 
Domain Context
CATH Clusters
| Superfamily | alpha/beta hydrolase | 
| Functional Family | Dipeptidyl peptidase 4 | 
Enzyme Information
| 3.4.21.- | 
							 Serine endopeptidases. 
							based on mapping to UniProt Q12884 		
							
							
						 | 
					
| 3.4.14.5 | 
							 Dipeptidyl-peptidase IV. 
							based on mapping to UniProt Q12884 		
							Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline. 
							-!- A membrane-bound serine-type peptidase in mammals. -!- EC 3.4.14.11 catalyzes a similar reaction. -!- Belongs to peptidase family S9B. 
						 | 
					
| 3.4.21.26 | 
							 Prolyl oligopeptidase. 
							based on mapping to UniProt Q12884 		
							Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides. 
							-!- Found in vertebrates, plants and Flavobacterium. -!- Generally cytosolic, commonly activated by thiol compounds. -!- Belongs to peptidase family S9A. -!- Formerly EC 3.4.22.18. 
						 | 
					
UniProtKB Entries (1)
| Q12884 | 
						 SEPR_HUMAN 
						Homo sapiens 
						Prolyl endopeptidase FAP 
					 | 
				
PDB Structure
| PDB | 1Z68 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Spodoptera | 
| Primary Citation | 
					 Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha. 
					    
					    J.Biol.Chem. 
					    
					 | 
			
