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Structure paper

TitleStructural and functional analysis of PucM, a hydrolase in the ureide pathway and a member of the transthyretin-related protein family.
Journal, issue, pagesProc. Natl. Acad. Sci. Usa, Vol. 103, Page 9790-9795, Year 2006
Publish dateMay 14, 2006 (structure data deposition date)
AuthorsJung, D.-K. / Lee, Y. / Park, S.G. / Park, B.C. / Kim, G.-H. / Rhee, S.
External linksProc. Natl. Acad. Sci. Usa / PubMed:16782815
MethodsX-ray diffraction
Resolution2.2 - 2.9 Å
Structure data

PDB-2h0e:
Crystal Structure of PucM in the absence of substrate
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-2h0f:
Crystal Structure of PucM in the presence of 8-azaxanthine
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-2h0j:
Crystal structure of PucM in the presence of 5,6-diaminouracil
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

ChemComp-AZA:
8-AZAXANTHINE

ChemComp-URN:
5,6-DIAMINOPYRIMIDINE-2,4(1H,3H)-DIONE

Source
  • bacillus subtilis (bacteria)
KeywordsHYDROLASE / BETA SANDWITCH / HIU / INHIBITOR COMPLEX / COMPLEX WITH DIAMINOURACIL

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