4Q3Y
Crystal structure of C. violaceum phenylalanine hydroxylase D139A mutation
Summary for 4Q3Y
| Entry DOI | 10.2210/pdb4q3y/pdb |
| Related | 1LTZ 3TK4 4Q3W 4Q3X 4Q3Z |
| Descriptor | Phenylalanine-4-hydroxylase, COBALT (II) ION (3 entities in total) |
| Functional Keywords | mutation, hydroxylase, phenylalanine hydroxylase, chromobacterium, kinetics, metals, phenylketonurias, biopterin, mixed alpha helix-beta sheet, oxidoreductase |
| Biological source | Chromobacterium violaceum |
| Total number of polymer chains | 1 |
| Total formula weight | 33661.94 |
| Authors | Ronau, J.A.,Abu-Omar, M.M.,Das, C. (deposition date: 2014-04-12, release date: 2015-02-18, Last modification date: 2023-09-20) |
| Primary citation | Ronau, J.A.,Paul, L.N.,Fuchs, J.E.,Liedl, K.R.,Abu-Omar, M.M.,Das, C. A conserved acidic residue in phenylalanine hydroxylase contributes to cofactor affinity and catalysis. Biochemistry, 53:6834-6848, 2014 Cited by PubMed: 25295853DOI: 10.1021/bi500734h PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.4 Å) |
Structure validation
Download full validation report
