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Structure paper

TitleStructural basis for the inhibition of human angiotensin-1 converting enzyme by fosinoprilat.
Journal, issue, pagesFebs J., Vol. 289, Page 6659-6671, Year 2022
Publish dateMar 14, 2022 (structure data deposition date)
AuthorsCozier, G.E. / Newby, E.C. / Schwager, S.L.U. / Isaac, R.E. / Sturrock, E.D. / Acharya, K.R.
External linksFebs J. / PubMed:35653492
MethodsX-ray diffraction
Resolution1.75 - 1.85 Å
Structure data

PDB-7z6z:
Crystal structure of Angiotensin-1 converting enzyme N-domain in complex with fosinoprilat
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

PDB-7z70:
Crystal structure of Angiotensin-1 converting enzyme C-domain in complex with fosinoprilat
Method: X-RAY DIFFRACTION / Resolution: 1.85 Å

Chemicals

ChemComp-KS8:
fosinoprilat / inhibitor*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM

ChemComp-ACT:
ACETATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-ZN:
Unknown entry

ChemComp-CL:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

ChemComp-BO3:
BORIC ACID

ChemComp-IMD:
IMIDAZOLE

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Angiotensin-1 converting enzyme / fosinoprilat / fosinopril / Metalloprotease

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