Iron in PDB 1pah: Human Phenylalanine Hydroxylase Dimer, Residues 117-424

All present enzymatic activity of Human Phenylalanine Hydroxylase Dimer, Residues 117-424:
1.14.16.1;

The structure of Human Phenylalanine Hydroxylase Dimer, Residues 117-424, PDB code: 1pah was solved by R.C.Stevens, H.Erlandsen, 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 (°)	66.600, 108.400, 125.700, 90.00, 90.00, 90.00
R / Rfree (%)	17.6 / 21.8

The binding sites of Iron atom in the Human Phenylalanine Hydroxylase Dimer, Residues 117-424 (pdb code 1pah). 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 Human Phenylalanine Hydroxylase Dimer, Residues 117-424, PDB code: 1pah:

Iron binding site 1 out of 1 in the Human Phenylalanine Hydroxylase Dimer, Residues 117-424


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Phenylalanine Hydroxylase Dimer, Residues 117-424 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe425 b:30.5 occ:1.00 OE2 A:GLU330 2.1 26.3 1.0 NE2 A:HIS290 2.2 23.5 1.0 NE2 A:HIS285 2.2 21.4 1.0 O A:HOH428 2.3 20.0 1.0 O A:HOH427 2.3 34.6 1.0 O A:HOH426 2.3 41.5 1.0 CD A:GLU330 3.1 27.1 1.0 CD2 A:HIS285 3.1 19.9 1.0 CE1 A:HIS290 3.1 18.9 1.0 CD2 A:HIS290 3.1 21.7 1.0 CE1 A:HIS285 3.2 21.7 1.0 OE1 A:GLU330 3.5 32.9 1.0 OE1 A:GLU286 4.2 21.8 1.0 ND1 A:HIS290 4.3 22.7 1.0 ND1 A:HIS285 4.3 24.9 1.0 CG A:HIS285 4.3 22.6 1.0 CG A:HIS290 4.3 21.8 1.0 CG A:GLU330 4.4 24.1 1.0 OH A:TYR325 4.5 31.1 1.0 CB A:ALA345 4.7 15.8 1.0 CB A:PRO281 4.8 26.1 1.0 CZ A:PHE263 4.9 26.3 1.0 O A:HOH451 4.9 40.3 1.0

H.Erlandsen, F.Fusetti, A.Martinez, E.Hough, T.Flatmark, R.C.Stevens. Crystal Structure of the Catalytic Domain of Human Phenylalanine Hydroxylase Reveals the Structural Basis For Phenylketonuria. Nat.Struct.Biol. V. 4 995 1997.
ISSN: ISSN 1072-8368
PubMed: 9406548
DOI: 10.1038/NSB1297-995