5mkt

X-ray diffraction
3.2Å resolution

Crystal structure of mouse prorenin

Released:
Source organism: Mus musculus
Entry authors: Yan Y, Read R

Function and Biology Details

Reaction catalysed:
Cleavage of Leu-|- bond in angiotensinogen to generate angiotensin I.
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Renin-1 Chain: A
Molecule details ›
Chain: A
Length: 389 amino acids
Theoretical weight: 42.78 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P06281 (Residues: 22-402; Coverage: 100%)
Gene names: Ren, Ren-1, Ren1
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: I41
Unit cell:
a: 141.232Å b: 141.232Å c: 82.961Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.265 0.263 0.297
Expression system: Homo sapiens