1pah

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Image:1pah.gif

1pah, resolution 2.0Å

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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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