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TitleProbing erectile function: S-(2-boronoethyl)-L-cysteine binds to arginase as a transition state analogue and enhances smooth muscle relaxation in human penile corpus cavernosum.
Journal, issue, pagesBiochemistry, Vol. 40, Page 2678-2688, Year 2001
Publish dateDec 14, 2000 (structure data deposition date)
AuthorsKim, N.N. / Cox, J.D. / Baggio, R.F. / Emig, F.A. / Mistry, S.K. / Harper, S.L. / Speicher, D.W. / Morris Jr., S.M. / Ash, D.E. / Traish, A. / Christianson, D.W.
External linksBiochemistry / PubMed:11258879
MethodsX-ray diffraction
Resolution2.3 Å
Structure data

PDB-1hq5:
CRYSTAL STRUCTURE OF THE BINUCLEAR MANGANESE METALLOENZYME ARGINASE COMPLEXED WITH S-(2-BORONOETHYL)-L-CYSTEINE, AN L-ARGININE ANALOGUE
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-S2C:
S-2-(BORONOETHYL)-L-CYSTEINE

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsHYDROLASE / BINUCLEAR MANGANESE CLUSTER / BORONIC ACID INHIBITOR / PERFECTLY TWINNED CRYSTAL

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