_EC 3.4.13.19 Membrane dipeptidase. 4 PDB entries  
EC 3.-.-.- Hydrolases. [20,887 PDB entries]
EC 3.4.-.- Acting on peptide bonds (peptide hydrolases). [6,819 PDB entries]
EC 3.4.13.- Dipeptidases. [25 PDB entries]
EC 3.4.13.19 Membrane dipeptidase. [4 PDB entries]    
1itq

Reaction: Hydrolysis of dipeptides.
Other name(s): Dehydropeptidase I. Dph i. Microsomal dipeptidase. Renal dipeptidase.
Cofactor(s): Zinc.
Comments: Membrane bound, with broad specificity. Abundant in the kidney cortex. Inhibited by bestatin and cilastatin. Belongs to peptidase family M19. Formerly Ec 3.4.3.1, Ec 3.4.3.2, Ec 3.4.3.6, Ec 3.4.13.1, Ec 3.4.13.2, Ec 3.4.13.8, Ec 3.4.13.11 and Ec 3.4.13.15.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 4 PDB entries in enzyme class E.C.3.4.13.19

  PDB code Protein
1itq
Human renal dipeptidase
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: renal cortex. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (369 residues) CATH domain: 3.20.20.140
1itu
Human renal dipeptidase complexed with cilastatin
Source: Homo sapiens. Human. Organism_taxid: 9606. Tissue: renal cortex. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Chains: A, B (369 residues) CATH domain: 3.20.20.140
3fdg
The crystal structure of the dipeptidase ac, metallo peptida family m19
Source: Rhodobacter sphaeroides. Organism_taxid: 272943. Strain: 2.4.1. Gene: gi:77388796, rhos4_24130, rsp_0802. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (338 residues) CATH domain: 3.20.20.140
3ly0
Crystal structure of metallo peptidase from rhodobacter sphaeroides liganded with phosphinate mimic of dipeptide l- ala-d-ala
Source: Rhodobacter sphaeroides. Organism_taxid: 272943. Strain: atcc 17023 / 2.4.1 / ncib 8253 / dsm 158. Gene: rhos4_24130, rsp_0802. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (351 residues) CATH domain: 3.20.20.140