1pah

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spinqualitylabelsall models 1pah, resolution 2.0Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

HUMAN PHENYLALANINE HYDROXYLASE DIMER, RESIDUES 117-424

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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.

Disease

Known diseases associated with this structure: Hyperphenylalaninemia, mild OMIM:[261600], Phenylketonuria OMIM:[261600]

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

Page seeded by OCA on Mon Nov 12 18:41:41 2007