8vju

X-ray diffraction
1.99Å resolution

Structure of Human Neurolysin in complex with dynorphin A13 peptide

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-272030 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Neurolysin, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 667 amino acids
Theoretical weight: 76.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BYT8 (Residues: 38-704; Coverage: 95%)
Gene names: AGTBP, KIAA1226, NLN
Sequence domains: Peptidase family M3
Dynorphin A(1-13) Chain: C
Molecule details ›
Chain: C
Length: 13 amino acids
Theoretical weight: 1.61 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P01213 (Residues: 207-219; Coverage: 6%)
Gene name: PDYN

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21212
Unit cell:
a: 142.067Å b: 60.257Å c: 95.553Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.218
Expression systems:
  • Escherichia coli
  • Not provided