› 2i4q

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
Cleavage of Leu-|- bond in angiotensinogen to generate angiotensin I.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133568 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Renin Chains: A, B
Molecule details ›
Chains: A, B
Length: 336 amino acids
Theoretical weight: 36.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00797 (Residues: 72-406; Coverage: 88%)
Gene name: REN
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand UA4 2 x UA4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P213
Unit cell:
a: 141.898Å b: 141.898Å c: 141.898Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.229 0.261
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Recent syntheses of 1,2,3,4-tetrahydroquinolines, 2,3-dihydro-4(1H)-quinolinones and 4(1H)-quinolinones using domino reactions.
Nammalwar et al. (2013)
1 more

1 mention without citation

Partial Characterization of Two Cathepsin D Family Aspartic Peptidases of Clonorchis sinensis.
Kang et al. (2019)