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Structure paper

TitleExploration of zinc-binding groups for the design of inhibitors for the oxytocinase subfamily of M1 aminopeptidases.
Journal, issue, pagesBioorg. Med. Chem., Vol. 27, Page 115177-115177, Year 2019
Publish dateApr 12, 2019 (structure data deposition date)
AuthorsTsoukalidou, S. / Kakou, M. / Mavridis, I. / Koumantou, D. / Calderone, V. / Fragai, M. / Stratikos, E. / Papakyriakou, A. / Vourloumis, D.
External linksBioorg. Med. Chem. / PubMed:31711716
MethodsX-ray diffraction
Resolution1.9 - 2.2 Å
Structure data

PDB-6rd0:
Human MMP12 catalytic domain in complex with AP280
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-6rly:
Human MMP12 (catalytic domain) in complex with AP316
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-CA:
Unknown entry

ChemComp-K0Q:
~{N}-[2-(1~{H}-indol-3-yl)ethyl]-2-(3-oxidanyl-2-oxidanylidene-pyridin-1-yl)ethanamide

ChemComp-HAE:
ACETOHYDROXAMIC ACID / inhibitor, medication*YM

ChemComp-HOH:
WATER

ChemComp-K8T:
2-(3-oxidanyl-2-oxidanylidene-pyridin-1-yl)-~{N}-[2-(4-phenylphenyl)ethyl]ethanamide

Source
  • homo sapiens (human)
KeywordsHYDROLASE / MMP12 / inhibitors / catalytic domain

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