› 1smr

X-ray diffraction
2Å resolution

The 3-d structure of mouse submaxillary renin complexed with a decapeptide inhibitor ch-66 based on the 4-16 fragment of rat angiotensinogen

Released:
DOI: 10.2210/pdb1smr/pdb
PDB entry 1smr coloured by chain, front view.
PDB entry 1smr coloured by chain, side view.
PDB entry 1smr coloured by chain, top view.
Source organisms:
Primary publication:
X-ray analysis at 2.0 A resolution of mouse submaxillary renin complexed with a decapeptide inhibitor CH-66, based on the 4-16 fragment of rat angiotensinogen.
Dealwis CG, Frazao C, Badasso M, Cooper JB, Tickle IJ, Driessen H, Blundell TL, Murakami K, Miyazaki H, Sueiras-Diaz J
J Mol Biol 236 342-60 (1994)
PMID: 8107115

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 domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
homo tetramer
monomeric
hetero octamer
hetero tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-133561 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Renin-2 Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 335 amino acids
Theoretical weight: 36.53 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P00796 (Residues: 67-401; Coverage: 89%)
Gene names: Ren-2, Ren2
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
Angiotensin 1-9 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 9 amino acids
Theoretical weight: 1.26 KDa
Source organism: Rattus norvegicus
Expression system: Not provided
UniProt:
  • Canonical: P01015 (Residues: 30-38; Coverage: 2%)
Gene names: Agt, Serpina8

Ligands and Environments

No bound ligands
2 modified residues:
Ligand PIV 4 x PIV
Ligand LPL 4 x LPL

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 78.34Å b: 117.76Å c: 85.88Å
α: 90° β: 101.18° γ: 90°
R-values:
R R work R free
0.18 not available not available
Expression system: Not provided

Quick links

Citations

1 review citation

The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides.
Siligardi et al. (1995)
15 other articles

7 mentions without citation

Mechanisms of Proteolytic Enzymes and Their Inhibition in QM/MM Studies.
Elsässer et al. (2021)
6 more