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Structure paper

TitleA Commensal Dipeptidyl Aminopeptidase with Specificity for N-Terminal Glycine Degrades Human-Produced Antimicrobial Peptides in Vitro.
Journal, issue, pagesAcs Chem. Biol., Vol. 13, Page 2513-2521, Year 2018
Publish dateJul 5, 2017 (structure data deposition date)
AuthorsXu, J.H. / Jiang, Z. / Solania, A. / Chatterjee, S. / Suzuki, B. / Lietz, C.B. / Hook, V.Y.H. / O'Donoghue, A.J. / Wolan, D.W.
External linksAcs Chem. Biol. / PubMed:30085657
MethodsX-ray diffraction
Resolution2.36 - 2.625 Å
Structure data

PDB-5wdk:
A processive dipeptidyl aminopeptidase secreted from an established commensal bacterium P. distasonis
Method: X-RAY DIFFRACTION / Resolution: 2.36 Å

PDB-5wdl:
A processive dipeptidyl aminopeptidase secreted from an established commensal bacterium P. distasonis
Method: X-RAY DIFFRACTION / Resolution: 2.625 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-T1O:
5-[(3aS,4R,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-N-(2-oxopropyl)pentanamide

ChemComp-HOH:
WATER

ChemComp-R33:
N-[(3S)-6-carbamimidamido-2-oxohexan-3-yl]glycinamide

Source
  • parabacteroides distasonis (strain atcc 8503 / dsm 20701 / cip 104284 / jcm 5825 / nctc 11152) (bacteria)
KeywordsHYDROLASE / Protease

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