_EC 3.4.24.16 Neurolysin. 3 PDB entries  
EC 3.-.-.- Hydrolases. [17,508 PDB entries]
EC 3.4.-.- Acting on peptide bonds (peptide hydrolases). [5,631 PDB entries]
EC 3.4.24.- Metalloendopeptidases. [517 PDB entries]
EC 3.4.24.16 Neurolysin. [3 PDB entries]    
1i1i

Reaction: Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.
Other name(s): Neurotensin endopeptidase.
Cofactor(s): Zn(2+).
Comments: No absolute requirement for a prolyl bond; the enzyme acts on some peptides, such as dynorphin 1-8, that do not contain proline, and does not act on some others that do. Belongs to peptidase family M3.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 3 PDB entries in enzyme class E.C.3.4.24.16

  PDB code Protein
1i1i
Neurolysin (endopeptidase 24.16) crystal structure
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: P (665 residues) CATH domains: 1.20.1050.40 3.40.390.10 1.10.1370.10
2o3e
Crystal structure of engineered neurolysin with thimet oligopeptidase specificity for neurotensin cleavage site.
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Gene: nln. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (665 residues) CATH domains: 1.20.1050.40 1.10.1370.10 3.40.390.10
4fxy
Crystal structure of rat neurolysin with bound pyrazolidin i
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: nln. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: P, Q (664 residues) CATH domains: 1.20.1050.40 1.10.1370.10 3.40.390.10