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-Structure paper
Title | A single active-site mutation of P450BM-3 dramatically enhances substrate binding and rate of product formation. |
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Journal, issue, pages | Biochemistry, Vol. 50, Page 8333-8341, Year 2011 |
Publish date | May 12, 2005 (structure data deposition date) |
![]() | Haines, D.C. / Hegde, A. / Chen, B. / Zhao, W. / Bondlela, M. / Humphreys, J.M. / Mullin, D.A. / Tomchick, D.R. / Machius, M. / Peterson, J.A. |
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Methods | X-ray diffraction |
Resolution | 1.46 - 1.74 Å |
Structure data | ![]() PDB-1zo4: ![]() PDB-1zoa: |
Chemicals | ![]() ChemComp-HEM: ![]() ChemComp-MES: ![]() ChemComp-GOL: ![]() ChemComp-HOH: ![]() ChemComp-140: |
Source |
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![]() | OXIDOREDUCTASE / cytochrome P-450 / Hemeprotein A328S / Hemeprotein A328V |