Function and Biology

RENIN IN COMPLEXED WITH 4-methoxy-3-(3-methoxypropoxy)-N-{[(3S,4S)-4-{[(4-methylphenyl)sulfonyl]amino}pyrrolidin-3-yl]methyl}-N-(propan-2-yl)benzamide INHIBITOR

Source organism: Homo sapiens
Biochemical function: aspartic-type endopeptidase activity
Biological process: proteolysis
Cellular component: not assigned

EC 3.4.23.15: Renin

Reaction catalysed:
Cleavage of Leu-|- bond in angiotensinogen to generate angiotensin I.
Alternative Name(s):
  • Angiotensin-forming enzyme
  • Angiotensinogenase

GO terms

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Sequence family

Pfam Protein family (Pfam)
PF00026
Domain description: Eukaryotic aspartyl protease
Occurring in:
  1. Renin
The deposited structure of PDB entry 4ryc contains 2 copies of Pfam domain PF00026 (Eukaryotic aspartyl protease) in Renin. Showing 1 copy in chain A.

InterPro InterPro annotations
IPR001461
Domain description: Aspartic peptidase A1 family
Occurring in:
  1. Renin
IPR021109
Domain description: Aspartic peptidase domain superfamily
Occurring in:
  1. Renin
IPR001969
Domain description: Aspartic peptidase, active site
Occurring in:
  1. Renin
IPR033121
Domain description: Peptidase family A1 domain
Occurring in:
  1. Renin
IPR034135
Domain description: Renin-like domain
Occurring in:
  1. Renin

Structure domain

CATH CATH domain
2.40.70.10
Class: Mainly Beta
Architecture: Beta Barrel
Topology: Cathepsin D, subunit A; domain 1
Homology: Acid Proteases
Occurring in:
  1. Renin
The deposited structure of PDB entry 4ryc contains 4 copies of CATH domain 2.40.70.10 (Cathepsin D, subunit A; domain 1) in Renin. Showing 2 copies in chain A.