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Structure paper

TitleStructures of neutrophil serine protease 4 reveal an unusual mechanism of substrate recognition by a trypsin-fold protease.
Journal, issue, pagesStructure, Vol. 22, Page 1333-1340, Year 2014
Publish dateApr 25, 2014 (structure data deposition date)
AuthorsLin, S.J. / Dong, K.C. / Eigenbrot, C. / van Lookeren Campagne, M. / Kirchhofer, D.
External linksStructure / PubMed:25156428
MethodsX-ray diffraction
Resolution1.4 - 3.07 Å
Structure data

PDB-4q7x:
Neutrophil serine protease 4 (PRSS57) apo form 1
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

PDB-4q7y:
Neutrophil serine protease 4 (PRSS57) apo form 2
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-4q7z:
Neutrophil serine protease 4 (PRSS57) with phe-phe-arg-chloromethylketone (FFR-cmk)
Method: X-RAY DIFFRACTION / Resolution: 1.4 Å

PDB-4q80:
Neutrophil serine protease 4 (PRSS57) with val-leu-lys-chloromethylketone (VLK-cmk)
Method: X-RAY DIFFRACTION / Resolution: 3.07 Å

Chemicals

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

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-2YT:
L-phenylalanyl-N-[(2S,3S)-6-carbamimidamido-1-chloro-2-hydroxyhexan-3-yl]-L-phenylalaninamide

ChemComp-2YS:
D-valyl-N-[(2S,3S)-7-amino-1-chloro-2-hydroxyheptan-3-yl]-L-leucinamide

Source
  • homo sapiens (human)
KeywordsHYDROLASE / trypsin homology / peptidase / HYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR complex

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