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Structure paper

TitleStructures and mechanism of dipeptidyl peptidases 8 and 9, important players in cellular homeostasis and cancer.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 115, Page E1437-E1445, Year 2018
Publish dateOct 10, 2017 (structure data deposition date)
AuthorsRoss, B. / Krapp, S. / Augustin, M. / Kierfersauer, R. / Arciniega, M. / Geiss-Friedlander, R. / Huber, R.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:29382749
MethodsX-ray diffraction
Resolution2.4 - 3.5 Å
Structure data

PDB-6eoo:
DPP8 - Apo, space group 20
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-6eop:
DPP8 - SLRFLYEG, space group 20
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-6eoq:
DPP9 - Apo
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-6eor:
DPP9 - 1G244
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-6eos:
DPP8 - Apo, space group 19
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-6eot:
DPP8 - SLRFLYEG, space group 19
Method: X-RAY DIFFRACTION / Resolution: 3.5 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-FLC:
CITRATE ANION

ChemComp-CA:
Unknown entry

ChemComp-F15:
PENTADECANOIC ACID

ChemComp-9XH:
(2~{S})-2-azanyl-4-[4-[bis(4-fluorophenyl)methyl]piperazin-1-yl]-1-(1,3-dihydroisoindol-2-yl)butane-1,4-dione

Source
  • homo sapiens (human)
KeywordsHYDROLASE / DPP8 / DPP9

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