1PAH
HUMAN PHENYLALANINE HYDROXYLASE DIMER, RESIDUES 117-424
Summary for 1PAH
| Entry DOI | 10.2210/pdb1pah/pdb |
| Descriptor | PHENYLALANINE HYDROXYLASE, FE (III) ION (3 entities in total) |
| Functional Keywords | oxidoreductase, phenylalanine, hydroxylase, phenylketonuria, pku |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 35756.36 |
| Authors | Stevens, R.C.,Erlandsen, H. (deposition date: 1997-10-25, release date: 1999-01-13, Last modification date: 2024-05-22) |
| Primary citation | Erlandsen, H.,Fusetti, F.,Martinez, A.,Hough, E.,Flatmark, T.,Stevens, R.C. Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nat.Struct.Biol., 4:995-1000, 1997 Cited by PubMed Abstract: The 2.0 A crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals a fold similar to that of tyrosine hydroxylase. It provides the first structural view of where mutations occur and a rationale to explain molecular mechanisms of the enzymatic phenotypes in the autosomal recessive disorder phenylketoneuria. PubMed: 9406548DOI: 10.1038/nsb1297-995 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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