› 2o3e

X-ray diffraction
2.2Å resolution

Crystal structure of engineered neurolysin with thimet oligopeptidase specificity for neurotensin cleavage site.

Released:
DOI: 10.2210/pdb2o3e/pdb
PDB entry 2o3e coloured by chain, front view.
PDB entry 2o3e coloured by chain, side view.
PDB entry 2o3e coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Swapping the substrate specificities of the neuropeptidases neurolysin and thimet oligopeptidase.
Lim EJ, Sampath S, Coll-Rodriguez J, Schmidt J, Ray K, Rodgers DW
J Biol Chem 282 9722-9732 (2007)
PMID: 17251185

Function and Biology Details

Reaction catalysed: 
Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154844 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neurolysin, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 678 amino acids
Theoretical weight: 77.64 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P42676 (Residues: 24-701; Coverage: 96%)
Gene name: Nln
Sequence domains: Peptidase family M3
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 159.55Å b: 87.7Å c: 58.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.268
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Commercial proteases: present and future.
Li et al. (2013)
3 more

1 mention without citation

Modeling SARS-CoV-2 spike/ACE2 protein-protein interactions for predicting the binding affinity of new spike variants for ACE2, and novel ACE2 structurally related human protein targets, for COVID-19 handling in the 3PM context.
Tragni et al. (2022)