PDBe 3vcm

X-ray diffraction
2.93Å resolution

Crystal structure of human prorenin

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Renin Chains: A, B
Molecule details ›
Chains: A, B
Length: 335 amino acids
Theoretical weight: 36.72 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P00797 (Residues: 67-406; Coverage: 88%)
  • Best match: P00797-2 (Residues: 67-403)
Gene name: REN
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Renin Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 43 amino acids
Theoretical weight: 5.12 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P00797 (Residues: 24-66; Coverage: 11%)
Gene name: REN
Sequence domains: A1 Propeptide

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P4322
Unit cell:
a: 104.42Å b: 104.42Å c: 237.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.212 0.248
Expression system: Homo sapiens