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Atomistry » Iron » PDB 1mkq-1mpw » 1mmk » |
Iron in PDB 1mmk: Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase ((Feii)) Complexed with Tetrahydrobiopterin and ThienylalanineEnzymatic activity of Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase ((Feii)) Complexed with Tetrahydrobiopterin and Thienylalanine
All present enzymatic activity of Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase ((Feii)) Complexed with Tetrahydrobiopterin and Thienylalanine:
1.14.16.1; Protein crystallography data
The structure of Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase ((Feii)) Complexed with Tetrahydrobiopterin and Thienylalanine, PDB code: 1mmk
was solved by
O.A.Andersen,
T.Flatmark,
E.Hough,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase ((Feii)) Complexed with Tetrahydrobiopterin and Thienylalanine
(pdb code 1mmk). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase ((Feii)) Complexed with Tetrahydrobiopterin and Thienylalanine, PDB code: 1mmk: Iron binding site 1 out of 1 in 1mmkGo back to Iron Binding Sites List in 1mmk
Iron binding site 1 out
of 1 in the Crystal Structure of Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase ((Feii)) Complexed with Tetrahydrobiopterin and Thienylalanine
Mono view Stereo pair view
Reference:
O.A.Andersen,
A.J.Stokka,
T.Flatmark,
E.Hough.
2.0A Resolution Crystal Structures of the Ternary Complexes of Human Phenylalanine Hydroxylase Catalytic Domain with Tetrahydrobiopterin and 3-(2-Thienyl)-L-Alanine or L-Norleucine: Substrate Specificity and Molecular Motions Related to Substrate Binding J.Mol.Biol. V. 333 747 2003.
Page generated: Sat Aug 3 11:01:55 2024
ISSN: ISSN 0022-2836 PubMed: 14568534 DOI: 10.1016/J.JMB.2003.09.004 |
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