Iron in PDB 1phz: Structure of Phosphorylated Phenylalanine Hydroxylase

All present enzymatic activity of Structure of Phosphorylated Phenylalanine Hydroxylase:
1.14.16.1;

The structure of Structure of Phosphorylated Phenylalanine Hydroxylase, PDB code: 1phz was solved by B.Kobe, I.G.Jennings, C.M.House, B.J.Michell, R.G.Cotton, B.E.Kemp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	99.00 / 2.20
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	56.783, 56.783, 302.851, 90.00, 90.00, 90.00
R / Rfree (%)	22.3 / 29.7

The binding sites of Iron atom in the Structure of Phosphorylated Phenylalanine Hydroxylase (pdb code 1phz). 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 Structure of Phosphorylated Phenylalanine Hydroxylase, PDB code: 1phz:

Iron binding site 1 out of 1 in the Structure of Phosphorylated Phenylalanine Hydroxylase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Phosphorylated Phenylalanine Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:64.0 occ:1.00 NE2 A:HIS285 2.4 29.7 1.0 NE2 A:HIS290 2.6 22.1 1.0 OE1 A:GLU330 2.7 36.8 1.0 O A:HOH533 2.8 25.8 1.0 CE1 A:HIS285 3.1 24.2 1.0 CD A:GLU330 3.3 34.1 1.0 OE2 A:GLU330 3.4 39.8 1.0 CD2 A:HIS290 3.4 20.3 1.0 CE1 A:HIS290 3.6 15.6 1.0 CD2 A:HIS285 3.6 27.5 1.0 OH A:TYR325 4.1 33.3 1.0 ND1 A:HIS285 4.3 29.5 1.0 OE1 A:GLU286 4.5 26.9 1.0 CG A:HIS285 4.6 26.2 1.0 CG A:HIS290 4.6 15.8 1.0 CG A:GLU330 4.6 29.3 1.0 ND1 A:HIS290 4.7 20.2 1.0 CB A:ALA345 4.7 25.7 1.0 CE1 A:TYR325 4.9 27.5 1.0 CB A:PRO281 4.9 42.2 1.0 CG A:PRO281 4.9 43.1 1.0 CZ A:TYR325 5.0 31.1 1.0

B.Kobe, I.G.Jennings, C.M.House, B.J.Michell, K.E.Goodwill, B.D.Santarsiero, R.C.Stevens, R.G.Cotton, B.E.Kemp. Structural Basis of Autoregulation of Phenylalanine Hydroxylase. Nat.Struct.Biol. V. 6 442 1999.
ISSN: ISSN 1072-8368
PubMed: 10331871
DOI: 10.1038/8247