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Iron in PDB 1kw0: Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine

Enzymatic activity of Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine

All present enzymatic activity of Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine:
1.14.16.1;

Protein crystallography data

The structure of Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine, PDB code: 1kw0 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:

Resolution Low / High (Å) 10.00 / 2.50
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 65.172, 106.741, 123.440, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 26.7

Iron Binding Sites:

The binding sites of Iron atom in the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine (pdb code 1kw0). 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 Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine, PDB code: 1kw0:

Iron binding site 1 out of 1 in 1kw0

Go back to Iron Binding Sites List in 1kw0
Iron binding site 1 out of 1 in the Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Catalytic Domain of Human Phenylalanine Hydroxylase (Fe(II)) in Complex with Tetrahydrobiopterin and Thienylalanine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe428

b:34.1
occ:1.00
 NE2 A:HIS285 2.3 22.9 1.0
NE2 A:HIS290 2.3 24.3 1.0
OE2 A:GLU330 2.4 27.2 1.0
O A:HOH438 2.4 44.4 1.0
OE1 A:GLU330 2.6 31.3 1.0
CD A:GLU330 2.8 27.8 1.0
CD2 A:HIS290 3.1 22.6 1.0
CE1 A:HIS285 3.2 22.3 1.0
CD2 A:HIS285 3.3 21.4 1.0
O4 A:H4B429 3.4 31.4 1.0
CE1 A:HIS290 3.5 23.2 1.0
N5 A:H4B429 3.7 30.8 1.0
CE2 A:TIH430 4.2 18.9 1.0
C4 A:H4B429 4.2 32.4 1.0
O9 A:H4B429 4.3 33.2 1.0
CG A:HIS290 4.3 22.4 1.0
CG A:GLU330 4.3 26.5 1.0
CE1 A:TIH430 4.3 19.1 1.0
ND1 A:HIS285 4.3 21.6 1.0
CB A:ALA345 4.4 22.5 1.0
CG A:HIS285 4.4 21.7 1.0
C4A A:H4B429 4.5 32.1 1.0
ND1 A:HIS290 4.5 24.1 1.0
C9 A:H4B429 4.7 32.6 1.0
OE2 A:GLU286 4.9 20.5 1.0
C6 A:H4B429 4.9 31.4 1.0
SD A:TIH430 4.9 21.4 1.0

Reference:

O.A.Andersen, T.Flatmark, E.Hough. Crystal Structure of the Ternary Complex of the Catalytic Domain of Human Phenylalanine Hydroxylase with Tetrahydrobiopterin and 3-(2-Thienyl)-L-Alanine, and Its Implications For the Mechanism of Catalysis and Substrate Activation J.Mol.Biol. V. 320 1095 2002.
ISSN: ISSN 0022-2836
PubMed: 12126628
DOI: 10.1016/S0022-2836(02)00560-0
Page generated: Wed Jul 16 17:13:21 2025

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