1pah
From Proteopedia
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Revision as of 14:53, 5 November 2007
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HUMAN PHENYLALANINE HYDROXYLASE DIMER, RESIDUES 117-424
Overview
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.
About this Structure
1PAH is a Single protein structure of sequence from Homo sapiens with FE as ligand. The following page contains interesting information on the relation of 1PAH with [Phenylalanine Hydroxylase]. Active as Phenylalanine 4-monooxygenase, with EC number 1.14.16.1 Structure known Active Site: NUL. Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria., Erlandsen H, Fusetti F, Martinez A, Hough E, Flatmark T, Stevens RC, Nat Struct Biol. 1997 Dec;4(12):995-1000. PMID:9406548
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