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Structure paper

TitleAllosteric inhibition of aminopeptidase N functions related to tumor growth and virus infection.
Journal, issue, pagesSci Rep, Vol. 7, Page 46045-46045, Year 2017
Publish dateJun 27, 2016 (structure data deposition date)
AuthorsSantiago, C. / Mudgal, G. / Reguera, J. / Recacha, R. / Albrecht, S. / Enjuanes, L. / Casasnovas, J.M.
External linksSci Rep / PubMed:28393915
MethodsX-ray diffraction
Resolution2 - 2.6 Å
Structure data

PDB-5lds:
Structure of the porcine aminopeptidase N ectodomain
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-5lg6:
Structure of the deglycosylated porcine aminopeptidase N ectodomain
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-5lhd:
Structure of glycosylated human aminopeptidase N
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

Chemicals

ChemComp-ZN:
Unknown entry

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

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-EDO:
1,2-ETHANEDIOL

Source
  • sus scrofa (pig)
  • homo sapiens (human)
KeywordsHYDROLASE / CD13 / pAPN / aminopeptidase / Coronavirus / receptor / enzime / porcine aminopeptidase N / Human aminopeptidase N / metalloprotease

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