1pah
From Proteopedia
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| , resolution 2.0Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Phenylalanine 4-monooxygenase, with EC number 1.14.16.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. The following page contains interesting information on the relation of 1PAH with [Phenylalanine Hydroxylase]. 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 Sun Mar 30 22:57:08 2008
