› 3k1w

X-ray diffraction
1.5Å resolution

New Classes of Potent and Bioavailable Human Renin Inhibitors

Released:
DOI: 10.2210/pdb3k1w/pdb
PDB entry 3k1w coloured by chain, front view.
PDB entry 3k1w coloured by chain, side view.
PDB entry 3k1w coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
New classes of potent and bioavailable human renin inhibitors.
Remen L, Bezençon O, Richard-Bildstein S, Bur D, Prade L, Corminboeuf O, Boss C, Grisostomi C, Sifferlen T, Strickner P, Hess P, Delahaye S, Treiber A, Weller T, Binkert C, Steiner B, Fischli W
Bioorg Med Chem Lett 19 6762-5 (2009)
PMID: 19853442

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

Assemblies composition:
monomeric
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: 341 amino acids
Theoretical weight: 37.41 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P00797 (Residues: 67-406; Coverage: 89%)
Gene name: REN
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

5 bound ligands:
Ligand BFX 2 x BFX
Ligand FMT 2 x FMT
Ligand NAG 1 x NAG
Ligand CL 1 x CL
Ligand HSQ 1 x HSQ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 66.028Å b: 88.697Å c: 118.307Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.199 0.233
Expression system: Homo sapiens

Quick links

Citations

1 review citation

Recent progress on the discovery of non-peptidic direct renin inhibitors for the clinical management of hypertension.
Yokokawa F. (2013)
7 other articles

4 mentions without citation

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