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Structure paper

TitleMolecular Basis for Multiple Omapatrilat Binding Sites within the ACE C-Domain: Implications for Drug Design.
Journal, issue, pagesJ. Med. Chem., Vol. 61, Page 10141-10154, Year 2018
Publish dateJul 25, 2018 (structure data deposition date)
AuthorsCozier, G.E. / Arendse, L.B. / Schwager, S.L. / Sturrock, E.D. / Acharya, K.R.
External linksJ. Med. Chem. / PubMed:30372620
MethodsX-ray diffraction
Resolution1.37 - 1.8 Å
Structure data

PDB-6h5w:
Crystal structure of human Angiotensin-1 converting enzyme C-domain in complex with Omapatrilat.
Method: X-RAY DIFFRACTION / Resolution: 1.37 Å

PDB-6h5x:
Crystal structure of human Angiotensin-1 converting enzyme N-domain in complex with Omapatrilat.
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-FT8:
Omapatrilat

ChemComp-IMD:
IMIDAZOLE

ChemComp-BO3:
BORIC ACID

ChemComp-P6G:
HEXAETHYLENE GLYCOL / precipitant*YM

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

ChemComp-XPE:
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL / precipitant*YM

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-MG:
Unknown entry

ChemComp-PGE:
TRIETHYLENE GLYCOL

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Angiotensin-1 converting enzyme / ACE inhibitor / Omapatrilat / Vasopeptidase inhibitor

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