Iron in PDB 5fgj: Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453

All present enzymatic activity of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453:
1.14.16.1;

The structure of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453, PDB code: 5fgj was solved by A.B.Taylor, K.M.Roberts, P.F.Fitzpatrick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	101.48 / 3.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	96.768, 102.686, 202.966, 90.00, 90.00, 90.00
R / Rfree (%)	26.8 / 29.6

The structure of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453 also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Iron atom in the Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453 (pdb code 5fgj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453, PDB code: 5fgj:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:67.5 occ:1.00 NE2 A:HIS290 2.1 68.3 1.0 NE2 A:HIS285 2.3 67.5 1.0 OE1 A:GLU330 2.9 73.1 1.0 CD2 A:HIS285 3.0 67.5 1.0 CD2 A:HIS290 3.1 68.3 1.0 CE1 A:HIS290 3.1 68.3 1.0 OE2 A:GLU330 3.2 73.1 1.0 CD A:GLU330 3.4 73.1 1.0 CE1 A:HIS285 3.5 67.5 1.0 OE2 A:GLU286 3.9 66.1 1.0 OH A:TYR325 4.1 73.9 1.0 ND1 A:HIS290 4.2 68.3 1.0 CG A:HIS290 4.2 68.3 1.0 CG A:HIS285 4.3 67.5 1.0 ND1 A:HIS285 4.5 67.5 1.0 CB A:ALA345 4.6 71.0 1.0 CG A:GLU330 5.0 73.1 1.0 CD A:GLU286 5.0 66.1 1.0

Iron binding site 2 out of 4 in the Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:62.2 occ:1.00 NE2 B:HIS285 2.1 67.5 1.0 NE2 B:HIS290 2.7 67.2 1.0 OE1 B:GLU330 2.8 70.9 1.0 CD2 B:HIS285 3.0 67.5 1.0 OE2 B:GLU330 3.0 70.9 1.0 CE1 B:HIS285 3.2 67.5 1.0 CD B:GLU330 3.3 70.9 1.0 CD2 B:HIS290 3.6 67.2 1.0 CE1 B:HIS290 3.7 67.2 1.0 OE2 B:GLU286 4.2 66.3 1.0 CG B:HIS285 4.2 67.5 1.0 ND1 B:HIS285 4.3 67.5 1.0 OH B:TYR325 4.4 70.5 1.0 ND1 B:HIS290 4.8 67.2 1.0 CG B:HIS290 4.8 67.2 1.0 CG B:GLU330 4.8 70.9 1.0 CB B:PRO281 4.9 67.7 1.0 CB B:ALA345 4.9 70.0 1.0

Iron binding site 3 out of 4 in the Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:61.2 occ:1.00 NE2 C:HIS285 2.6 69.6 1.0 OE1 C:GLU330 2.7 73.1 1.0 NE2 C:HIS290 2.8 66.4 1.0 OE2 C:GLU330 3.0 73.1 1.0 CD C:GLU330 3.2 73.1 1.0 CD2 C:HIS285 3.3 69.6 1.0 CE1 C:HIS290 3.6 66.4 1.0 CE1 C:HIS285 3.7 69.6 1.0 CD2 C:HIS290 3.8 66.4 1.0 OE2 C:GLU286 4.2 69.0 1.0 OH C:TYR325 4.5 73.2 1.0 CG C:HIS285 4.6 69.6 1.0 CG C:GLU330 4.7 73.1 1.0 CB C:PRO281 4.7 72.6 1.0 ND1 C:HIS285 4.7 69.6 1.0 ND1 C:HIS290 4.8 66.4 1.0 CG C:PRO281 4.9 72.6 1.0 CG C:HIS290 4.9 66.4 1.0

Iron binding site 4 out of 4 in the Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Tetrameric Rat Phenylalanine Hydroxylase, Residues 1-453 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe501 b:78.7 occ:1.00 NE2 D:HIS290 2.5 78.2 1.0 NE2 D:HIS285 2.6 82.9 1.0 OE1 D:GLU330 2.8 82.8 1.0 OE2 D:GLU330 3.2 82.8 1.0 CE1 D:HIS290 3.3 78.2 1.0 CD2 D:HIS285 3.3 82.9 1.0 CD D:GLU330 3.4 82.8 1.0 CD2 D:HIS290 3.6 78.2 1.0 CE1 D:HIS285 3.8 82.9 1.0 OH D:TYR325 4.0 81.4 1.0 OE2 D:GLU286 4.1 81.2 1.0 ND1 D:HIS290 4.5 78.2 1.0 CG D:HIS285 4.6 82.9 1.0 CG D:HIS290 4.7 78.2 1.0 ND1 D:HIS285 4.8 82.9 1.0 CE1 D:TYR325 4.8 81.4 1.0 CG D:GLU330 4.9 82.8 1.0 CB D:PRO281 4.9 85.5 1.0 CZ D:TYR325 4.9 81.4 1.0 CB D:ALA345 4.9 82.9 1.0

S.P.Meisburger, A.B.Taylor, C.A.Khan, S.Zhang, P.F.Fitzpatrick, N.Ando. Domain Movements Upon Activation of Phenylalanine Hydroxylase Characterized By Crystallography and Chromatography-Coupled Small-Angle X-Ray Scattering. J.Am.Chem.Soc. V. 138 6506 2016.
ISSN: ESSN 1520-5126
PubMed: 27145334
DOI: 10.1021/JACS.6B01563