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-Structure paper
Title | A conserved active site tyrosine residue of proline dehydrogenase helps enforce the preference for proline over hydroxyproline as the substrate. |
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Journal, issue, pages | Biochemistry, Vol. 48, Page 951-959, Year 2009 |
Publish date | Aug 6, 2008 (structure data deposition date) |
![]() | Ostrander, E.L. / Larson, J.D. / Schuermann, J.P. / Tanner, J.J. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.75 - 2 Å |
Structure data | ![]() PDB-3e2q: ![]() PDB-3e2r: ![]() PDB-3e2s: |
Chemicals | ![]() ChemComp-FAD: ![]() ChemComp-HYP: ![]() ChemComp-1PE: ![]() ChemComp-HOH: ![]() ChemComp-TFB: ![]() ChemComp-CIT: ![]() ChemComp-PRO: |
Source |
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![]() | OXIDOREDUCTASE / Proline utilization A / PutA / flavoenzyme / DNA-binding / FAD / Flavoprotein / Multifunctional enzyme / NAD / Proline metabolism / Repressor / Transcription / Transcription regulation |