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-Structure paper
Title | A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis. |
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Journal, issue, pages | Biochemistry, Vol. 53, Page 6834-6848, Year 2014 |
Publish date | Apr 12, 2014 (structure data deposition date) |
Authors | Ronau, J.A. / Paul, L.N. / Fuchs, J.E. / Liedl, K.R. / Abu-Omar, M.M. / Das, C. |
External links | Biochemistry / PubMed:25295853 |
Methods | X-ray diffraction |
Resolution | 1.35 - 1.4 Å |
Structure data | PDB-4q3w: PDB-4q3x: PDB-4q3y: PDB-4q3z: |
Chemicals | ChemComp-CO: ChemComp-EDO: ChemComp-HOH: |
Source |
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Keywords | OXIDOREDUCTASE / Mutation / hydroxylase / phenylalanine hydroxylase / kinetics / metals / Chromobacterium / phenylketonurias / biopterin / Mixed alpha helix-beta sheet / phenylketonuria |