Iron in PDB 6n1k: Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State

All present enzymatic activity of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State:
1.14.16.1;

The structure of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State, PDB code: 6n1k was solved by E.C.Arturo, E.K.Jaffe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.29 / 3.06
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.437, 202.640, 72.574, 90.00, 90.30, 90.00
R / Rfree (%)	20.3 / 23.8

The structure of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State also contains other interesting chemical elements:

Chlorine

(Cl)

4 atoms

The binding sites of Iron atom in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State (pdb code 6n1k). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State, PDB code: 6n1k:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:1.0 occ:1.00 NE2 A:HIS290 2.2 95.3 1.0 O A:HOH602 2.2 0.9 1.0 NE2 A:HIS285 2.2 0.3 1.0 O A:HOH601 2.2 0.6 1.0 OE2 A:GLU330 2.2 70.6 1.0 CE1 A:HIS290 2.9 91.7 1.0 HE1 A:HIS290 3.0 0.0 1.0 CD A:GLU330 3.0 71.2 1.0 CE1 A:HIS285 3.1 0.7 1.0 OE1 A:GLU330 3.1 71.8 1.0 HE1 A:HIS285 3.2 0.7 1.0 CD2 A:HIS290 3.2 0.0 1.0 CD2 A:HIS285 3.2 0.4 1.0 HD2 A:HIS285 3.5 0.9 1.0 HD2 A:HIS290 3.5 0.8 1.0 HH A:TYR325 3.7 75.6 1.0 OE1 A:GLU286 3.8 70.0 1.0 ND1 A:HIS290 4.0 0.1 1.0 HB3 A:ALA345 4.1 0.1 1.0 CG A:HIS290 4.2 73.8 1.0 ND1 A:HIS285 4.2 0.1 1.0 HB3 A:PRO281 4.3 0.1 1.0 CG A:HIS285 4.4 97.9 1.0 HE2 A:TYR325 4.4 77.6 1.0 HB1 A:ALA345 4.4 0.1 1.0 CG A:GLU330 4.5 71.5 1.0 OH A:TYR325 4.5 63.0 1.0 HZ A:PHE263 4.6 96.5 1.0 CD A:GLU286 4.7 70.5 1.0 CB A:ALA345 4.7 85.1 1.0 HG2 A:GLU330 4.7 85.8 1.0 HD1 A:HIS290 4.7 0.9 1.0 HE1 A:PHE263 4.7 96.5 1.0 HG3 A:GLU330 4.8 85.8 1.0 OE2 A:GLU286 4.8 70.6 1.0

Iron binding site 2 out of 4 in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:0.7 occ:1.00 NE2 B:HIS285 2.1 0.9 1.0 O B:HOH602 2.2 0.4 1.0 NE2 B:HIS290 2.2 80.6 1.0 O B:HOH601 2.2 0.1 1.0 OE1 B:GLU330 2.2 87.4 1.0 CE1 B:HIS290 3.0 79.2 1.0 CD B:GLU330 3.0 88.0 1.0 CD2 B:HIS285 3.1 0.8 1.0 HE1 B:HIS290 3.1 95.1 1.0 OE2 B:GLU330 3.1 88.3 1.0 CE1 B:HIS285 3.2 0.1 1.0 CD2 B:HIS290 3.2 79.4 1.0 HD2 B:HIS285 3.2 0.4 1.0 HE1 B:HIS285 3.4 0.1 1.0 HD2 B:HIS290 3.4 95.3 1.0 OH B:TYR325 4.1 71.3 1.0 ND1 B:HIS290 4.1 78.2 1.0 HG2 B:GLU286 4.1 0.9 1.0 HB3 B:PRO281 4.2 86.8 1.0 CG B:HIS290 4.2 78.5 1.0 CG B:HIS285 4.2 0.1 1.0 ND1 B:HIS285 4.3 1.0 1.0 HB3 B:ALA345 4.3 93.5 1.0 CG B:GLU330 4.5 88.7 1.0 HE2 B:TYR325 4.5 87.7 1.0 HH B:TYR325 4.5 85.5 1.0 HZ B:PHE263 4.5 93.0 1.0 HE1 B:PHE263 4.6 92.1 1.0 HG2 B:GLU330 4.7 0.4 1.0 HG3 B:GLU330 4.8 0.4 1.0 HB1 B:ALA345 4.8 93.5 1.0 HD1 B:HIS290 4.8 93.9 1.0 CG B:GLU286 5.0 94.1 1.0

Iron binding site 3 out of 4 in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe502 b:0.4 occ:1.00 OE2 C:GLU330 2.1 0.1 1.0 NE2 C:HIS285 2.1 0.1 1.0 NE2 C:HIS290 2.2 67.1 1.0 O C:HOH601 2.2 0.4 1.0 OE1 C:GLU330 2.3 0.6 1.0 CD C:GLU330 2.5 0.8 1.0 CE1 C:HIS290 2.9 66.5 1.0 HE1 C:HIS290 2.9 79.8 1.0 CE1 C:HIS285 3.0 96.9 1.0 HE1 C:HIS285 3.1 0.3 1.0 CD2 C:HIS285 3.3 0.5 1.0 CD2 C:HIS290 3.4 66.9 1.0 HD2 C:HIS285 3.5 0.4 1.0 HH C:TYR325 3.6 82.2 1.0 HD2 C:HIS290 3.7 80.3 1.0 HB3 C:ALA345 3.9 96.1 1.0 CG C:GLU330 4.0 72.3 1.0 ND1 C:HIS290 4.1 65.9 1.0 ND1 C:HIS285 4.2 0.4 1.0 OH C:TYR325 4.3 68.5 1.0 CG C:HIS285 4.3 79.6 1.0 CG C:HIS290 4.4 66.1 1.0 HB1 C:ALA345 4.4 96.1 1.0 HB3 C:PRO281 4.5 0.7 1.0 HE2 C:TYR325 4.5 83.9 1.0 CB C:ALA345 4.6 80.0 1.0 HG2 C:GLU286 4.7 97.9 1.0 HZ C:PHE263 4.7 0.8 1.0 HG3 C:PRO281 4.7 0.8 1.0 HD1 C:HIS290 4.8 79.0 1.0 HD1 C:HIS285 4.9 0.2 1.0 CB C:GLU330 4.9 66.8 1.0 HB2 C:ALA345 5.0 96.1 1.0 HE1 C:PHE263 5.0 0.7 1.0

Iron binding site 4 out of 4 in the Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Full-Length Human Phenylalanine Hydroxylase (Pah) in the Resting State within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe502 b:0.5 occ:1.00 NE2 D:HIS285 2.2 75.8 1.0 OE2 D:GLU330 2.2 98.4 1.0 O D:HOH602 2.2 0.2 1.0 NE2 D:HIS290 2.2 72.0 1.0 O D:HOH601 2.2 99.8 1.0 CE1 D:HIS290 2.9 71.6 1.0 CD D:GLU330 3.0 99.4 1.0 CE1 D:HIS285 3.0 73.5 1.0 OE1 D:GLU330 3.2 100.0 1.0 CD2 D:HIS285 3.2 88.6 1.0 CD2 D:HIS290 3.2 71.7 1.0 HH D:TYR325 3.5 0.4 1.0 OE2 D:GLU286 3.9 82.3 1.0 ND1 D:HIS290 4.0 71.0 1.0 HB3 D:PRO281 4.2 0.8 1.0 CG D:HIS290 4.2 71.0 1.0 ND1 D:HIS285 4.2 89.1 1.0 CG D:HIS285 4.3 73.5 1.0 OH D:TYR325 4.3 0.2 1.0 HB3 D:ALA345 4.4 0.8 1.0 HE2 D:TYR325 4.4 0.3 1.0 CG D:GLU330 4.5 0.0 1.0 HZ D:PHE263 4.6 81.7 1.0 HG2 D:GLU330 4.7 0.0 1.0 CD D:GLU286 4.7 79.5 1.0 HE1 D:PHE263 4.7 81.4 1.0 HG3 D:GLU330 4.7 0.0 1.0 HB1 D:ALA345 4.8 0.8 1.0 OE1 D:GLU286 4.9 80.8 1.0

E.C.Arturo, K.Gupta, M.R.Hansen, E.Borne, E.K.Jaffe. Biophysical Characterization of Full-Length Human Phenylalanine Hydroxylase Provides A Deeper Understanding of Its Quaternary Structure Equilibrium. J.Biol.Chem. V. 294 10131 2019.
ISSN: ESSN 1083-351X
PubMed: 31076506
DOI: 10.1074/JBC.RA119.008294