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Structure paper

TitleCrystal Structures of ERAP2 Complexed with Inhibitors Reveal Pharmacophore Requirements for Optimizing Inhibitor Potency.
Journal, issue, pagesACS Med Chem Lett, Vol. 8, Page 333-337, Year 2017
Publish dateApr 5, 2016 (structure data deposition date)
AuthorsMpakali, A. / Giastas, P. / Deprez-Poulain, R. / Papakyriakou, A. / Koumantou, D. / Gealageas, R. / Tsoukalidou, S. / Vourloumis, D. / Mavridis, I.M. / Stratikos, E. / Saridakis, E.
External linksACS Med Chem Lett / PubMed:28337326
MethodsX-ray diffraction
Resolution2.8 - 2.897 Å
Structure data

PDB-5j6s:
Crystal structure of Endoplasmic Reticulum Aminopeptidase 2 (ERAP2) in complex with a hydroxamic derivative ligand
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-5k1v:
Crystal structure of Endoplasmic Reticulum aminopeptidase 2 (ERAP2) in complex with a diaminobenzoic acid derivative ligand.
Method: X-RAY DIFFRACTION / Resolution: 2.897 Å

Chemicals

ChemComp-ZN:
Unknown entry

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

ChemComp-6GA:
(2S)-N~1~-benzyl-2-[(4-fluorophenyl)methyl]-N~3~-hydroxypropanediamide

ChemComp-HOH:
WATER

ChemComp-6PX:
methyl N-[4-amino-3-(L-arginylamino)benzene-1-carbonyl]-L-tyrosinate

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Endoplasmic reticulum / aminopeptidase / Zn binding metallopeptidase / Endoplasmic Reticulum aminopeptidase / zinc-binding metallopeptidase / diaminobenzoic acid derivative

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