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-Structure paper
| Title | Structure-based dissection of the active site chemistry of leukotriene a4 hydrolase: implications for m1 aminopeptidases and inhibitor design. |
|---|---|
| Journal, issue, pages | Chem. Biol., Vol. 15, Page 920-929, Year 2008 |
| Publish date | Sep 3, 2007 (structure data deposition date) |
Authors | Tholander, F. / Muroya, A. / Roques, B.P. / Fournie-Zaluski, M.C. / Thunnissen, M.M. / Haeggstrom, J.Z. |
External links | Chem. Biol. / PubMed:18804029 |
| Methods | X-ray diffraction |
| Resolution | 1.465 - 2.3 Å |
| Structure data | ![]() PDB-2r59: ![]() PDB-3b7r: ![]() PDB-3b7s: ![]() PDB-3b7t: ![]() PDB-3b7u: |
| Chemicals | ![]() ChemComp-ZN: ![]() ChemComp-YB: ![]() ChemComp-PH0: ![]() ChemComp-ACY: ![]() ChemComp-HOH: ![]() ChemComp-IMD: ![]() ChemComp-BIR: ![]() ChemComp-GOL: ![]() ChemComp-KEL: |
| Source |
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Keywords | HYDROLASE / transition state / analogue peptide / hydrolysis / Alternative splicing / Cytoplasm / Leukotriene biosynthesis / Metal-binding / Metalloprotease / Multifunctional enzyme / Protease / Zinc / TRIPEPTIDE SUBSTRATE |
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homo sapiens (human)
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