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Structure paper

TitleProbing the role of the hyper-reactive histidine residue of arginase.
Journal, issue, pagesArch. Biochem. Biophys., Vol. 444, Page 15-26, Year 2005
Publish dateMay 19, 2004 (structure data deposition date)
AuthorsColleluori, D.M. / Reczkowski, R.S. / Emig, F.A. / Cama, E. / Cox, J.D. / Scolnick, L.R. / Compher, K. / Jude, K. / Han, S. / Viola, R.E. ...Colleluori, D.M. / Reczkowski, R.S. / Emig, F.A. / Cama, E. / Cox, J.D. / Scolnick, L.R. / Compher, K. / Jude, K. / Han, S. / Viola, R.E. / Christianson, D.W. / Ash, D.E.
External linksArch. Biochem. Biophys. / PubMed:16266687
MethodsX-ray diffraction
Resolution1.7 - 3.1 Å
Structure data

PDB-1ta1:
H141C mutant of rat liver arginase I
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-1tbh:
H141D mutant of rat liver arginase I
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-1tbj:
H141A mutant of rat liver arginase I
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

PDB-1tbl:
H141N mutant of rat liver arginase I
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-1zpe:
Arginase I covalently modified with butylamine at Q19C
Method: X-RAY DIFFRACTION / Resolution: 1.7 Å

PDB-1zpg:
Arginase I covalently modified with propylamine at Q19C
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsHYDROLASE / arginase / binuclear manganese cluster / H141C mutation / H141D / arginase I / H141A mutant / H141N mutant / chemically modified enzyme

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