6pah
From Proteopedia
|
HUMAN PHENYLALANINE HYDROXYLASE CATALYTIC DOMAIN DIMER WITH BOUND L-DOPA (3,4-DIHYDROXYPHENYLALANINE) INHIBITOR
Overview
The aromatic amino acid hydroxylases represent a superfamily of, structurally and functionally closely related enzymes, one of those, functions being reversible inhibition by catechol derivatives. Here we, present the crystal structure of the dimeric catalytic domain (residues, 117-424) of human phenylalanine hydroxylase (hPheOH), cocrystallized with, various potent and well-known catechol inhibitors and refined at a, resolution of 2.0 A. The catechols bind by bidentate coordination to each, iron in both subunits of the dimer through the catechol hydroxyl groups, forming a blue-green colored ligand-to-metal charge-transfer complex. In, addition, Glu330 and Tyr325 are identified as determinant residues in the, recognition of the inhibitors. In particular, the interaction with Glu330, ... [(full description)]
About this Structure
6PAH is a [Single protein] structure of sequence from [Homo sapiens] with FE and DAH as [ligands]. Active as [[1]], with EC number [1.14.16.1]. Full crystallographic information is available from [OCA].
Reference
Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution., Erlandsen H, Flatmark T, Stevens RC, Hough E, Biochemistry. 1998 Nov 10;37(45):15638-46. PMID:9843368
Page seeded by OCA on Mon Oct 29 19:08:09 2007
