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-Structure paper
Title | Probing the role of the hyper-reactive histidine residue of arginase. |
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Journal, issue, pages | Arch. Biochem. Biophys., Vol. 444, Page 15-26, Year 2005 |
Publish date | May 19, 2004 (structure data deposition date) |
![]() | 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. ...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. |
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Methods | X-ray diffraction |
Resolution | 1.7 - 3.1 Å |
Structure data | ![]() PDB-1ta1: ![]() PDB-1tbh: ![]() PDB-1tbj: ![]() PDB-1tbl: ![]() PDB-1zpe: ![]() PDB-1zpg: |
Chemicals | ![]() ChemComp-MN: ![]() ChemComp-GOL: ![]() ChemComp-HOH: |
Source |
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![]() | HYDROLASE / arginase / binuclear manganese cluster / H141C mutation / H141D / arginase I / H141A mutant / H141N mutant / chemically modified enzyme |