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-Structure paper
Title | Unprecedented access of phenolic substrates to the heme active site of a catalase: Substrate binding and peroxidase-like reactivity of Bacillus pumilus catalase monitored by X-ray crystallography and EPR spectroscopy. |
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Journal, issue, pages | Proteins, Vol. 83, Page 853-866, Year 2015 |
Publish date | Jun 20, 2014 (structure data deposition date) |
![]() | Loewen, P.C. / Villanueva, J. / Switala, J. / Donald, L.J. / Ivancich, A. |
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Methods | X-ray diffraction |
Resolution | 1.65 - 1.95 Å |
Structure data | ![]() PDB-4qol: ![]() PDB-4qom: ![]() PDB-4qon: ![]() PDB-4qoo: ![]() PDB-4qop: ![]() PDB-4qoq: ![]() PDB-4qor: |
Chemicals | ![]() ChemComp-HEM: ![]() ChemComp-CL: ![]() ChemComp-NA: ![]() ChemComp-ACT: ![]() ChemComp-HOH: ![]() ChemComp-PYG: ![]() ChemComp-CAQ: ![]() ChemComp-RCO: ![]() ChemComp-HQE: ![]() ChemComp-JZ3: ![]() ChemComp-2CH: |
Source |
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![]() | OXIDOREDUCTASE / catalase fold / catalase / peroxidase / catalase and peroxidase |