PDBe 1i1i

X-ray diffraction
2.3Å resolution

NEUROLYSIN (ENDOPEPTIDASE 24.16) CRYSTAL STRUCTURE

Released:
Source organism: Rattus norvegicus
Primary publication:
Structure of neurolysin reveals a deep channel that limits substrate access.
Proc. Natl. Acad. Sci. U.S.A. 98 3127-32 (2001)
PMID: 11248043

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neurolysin, mitochondrial Chain: P
Molecule details ›
Chain: P
Length: 681 amino acids
Theoretical weight: 77.87 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P42676 (Residues: 24-704; Coverage: 97%)
Gene name: Nln
Sequence domains: Peptidase family M3
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21212
Unit cell:
a: 157.6Å b: 87.7Å c: 58.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.268
Expression system: Escherichia coli