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Iron in PDB 1dmw: Crystal Structure of Double Truncated Human Phenylalanine Hydroxylase with Bound 7,8-Dihydro-L-Biopterin

Enzymatic activity of Crystal Structure of Double Truncated Human Phenylalanine Hydroxylase with Bound 7,8-Dihydro-L-Biopterin

All present enzymatic activity of Crystal Structure of Double Truncated Human Phenylalanine Hydroxylase with Bound 7,8-Dihydro-L-Biopterin:
1.14.16.1;

Protein crystallography data

The structure of Crystal Structure of Double Truncated Human Phenylalanine Hydroxylase with Bound 7,8-Dihydro-L-Biopterin, PDB code: 1dmw was solved by H.Erlandsen, R.C.Stevens, T.Flatmark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 66.357, 107.991, 124.591, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 24.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Double Truncated Human Phenylalanine Hydroxylase with Bound 7,8-Dihydro-L-Biopterin (pdb code 1dmw). 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 Double Truncated Human Phenylalanine Hydroxylase with Bound 7,8-Dihydro-L-Biopterin, PDB code: 1dmw:

Iron binding site 1 out of 1 in 1dmw

Go back to Iron Binding Sites List in 1dmw
Iron binding site 1 out of 1 in the Crystal Structure of Double Truncated Human Phenylalanine Hydroxylase with Bound 7,8-Dihydro-L-Biopterin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Double Truncated Human Phenylalanine Hydroxylase with Bound 7,8-Dihydro-L-Biopterin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe425

b:27.6
occ:1.00
 OE2 A:GLU330 2.0 32.5 1.0
NE2 A:HIS290 2.1 22.6 1.0
NE2 A:HIS285 2.2 25.0 1.0
O A:HOH567 2.2 34.0 1.0
O A:HOH459 2.3 25.5 1.0
O A:HOH528 2.6 47.5 1.0
CD A:GLU330 3.0 32.1 1.0
CE1 A:HIS290 3.0 19.5 1.0
CD2 A:HIS285 3.1 22.4 1.0
CD2 A:HIS290 3.1 22.8 1.0
CE1 A:HIS285 3.2 27.5 1.0
OE1 A:GLU330 3.3 37.4 1.0
O4 A:HBI700 3.8 37.8 0.5
ND1 A:HIS290 4.2 22.7 1.0
CG A:HIS290 4.2 22.3 1.0
CG A:GLU330 4.3 30.9 1.0
CG A:HIS285 4.3 26.6 1.0
ND1 A:HIS285 4.3 27.6 1.0
OE1 A:GLU286 4.4 24.8 1.0
CB A:ALA345 4.6 22.6 1.0
OH A:TYR325 4.7 29.5 1.0
O A:HOH449 4.8 33.7 1.0
CB A:PRO281 4.9 27.4 1.0

Reference:

H.Erlandsen, E.Bjorgo, T.Flatmark, R.C.Stevens. Crystal Structure and Site-Specific Mutagenesis of Pterin-Bound Human Phenylalanine Hydroxylase. Biochemistry V. 39 2208 2000.
ISSN: ISSN 0006-2960
PubMed: 10694386
DOI: 10.1021/BI992531+
Page generated: Wed Jul 16 13:22:01 2025

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