Iron in PDB 6zzu: Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th).

All present enzymatic activity of Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th).:
1.14.16.2;

The binding sites of Iron atom in the Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th). (pdb code 6zzu). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th)., PDB code: 6zzu:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th). within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:153.0 occ:1.00 NE2 B:HIS330 2.2 108.8 1.0 NE2 B:HIS335 2.2 112.9 1.0 O B:HOH601 2.4 130.3 1.0 OE2 B:GLU375 2.5 112.5 1.0 CD2 B:HIS335 2.6 112.9 1.0 CD2 B:HIS330 2.9 108.8 1.0 OE1 B:GLU375 3.0 112.5 1.0 CD B:GLU375 3.1 112.5 1.0 CE1 B:HIS330 3.3 108.8 1.0 CE1 B:HIS335 3.5 112.9 1.0 CG B:HIS335 4.0 112.9 1.0 CG B:HIS330 4.1 108.8 1.0 CB B:PRO326 4.2 107.5 1.0 ND1 B:HIS330 4.3 108.8 1.0 ND1 B:HIS335 4.3 112.9 1.0 CZ B:PHE308 4.5 111.5 1.0 CG B:GLU375 4.6 112.5 1.0 CB B:ALA390 4.7 113.0 1.0 CG B:PRO326 4.9 107.5 1.0 CE1 B:PHE308 5.0 111.5 1.0

Iron binding site 2 out of 4 in the Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th). within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:145.9 occ:1.00 NE2 A:HIS330 2.2 111.1 1.0 NE2 A:HIS335 2.2 114.8 1.0 O A:HOH601 2.4 117.2 1.0 CD2 A:HIS335 2.4 114.8 1.0 CD2 A:HIS330 2.6 111.1 1.0 OE2 A:GLU375 2.8 113.5 1.0 OE1 A:GLU375 3.3 113.5 1.0 CE1 A:HIS330 3.4 111.1 1.0 CD A:GLU375 3.5 113.5 1.0 CE1 A:HIS335 3.5 114.8 1.0 CG A:HIS335 3.8 114.8 1.0 CG A:HIS330 3.9 111.1 1.0 CB A:PRO326 4.1 108.8 1.0 ND1 A:HIS335 4.2 114.8 1.0 ND1 A:HIS330 4.3 111.1 1.0 CZ A:PHE308 4.3 116.1 1.0 CB A:GLU331 4.7 118.1 1.0 OE1 A:GLU331 4.8 118.1 1.0 CE1 A:PHE308 4.8 116.1 1.0 CG A:PRO326 4.8 108.8 1.0 CB A:ALA390 4.8 114.3 1.0 CG A:GLU375 4.9 113.5 1.0 CB A:HIS335 5.0 114.8 1.0

Iron binding site 3 out of 4 in the Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th). within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe500 b:160.6 occ:1.00 OE2 C:GLU375 2.1 118.3 1.0 NE2 C:HIS330 2.2 116.6 1.0 NE2 C:HIS335 2.2 114.9 1.0 O C:HOH601 2.5 127.0 1.0 CD2 C:HIS330 2.8 116.6 1.0 CD2 C:HIS335 2.8 114.9 1.0 CD C:GLU375 3.0 118.3 1.0 OE1 C:GLU375 3.1 118.3 1.0 CE1 C:HIS330 3.4 116.6 1.0 CE1 C:HIS335 3.4 114.9 1.0 CG C:HIS330 4.0 116.6 1.0 CG C:HIS335 4.0 114.9 1.0 CB C:PRO326 4.1 112.4 1.0 ND1 C:HIS330 4.3 116.6 1.0 ND1 C:HIS335 4.3 114.9 1.0 CG C:GLU375 4.4 118.3 1.0 CG C:PRO326 4.7 112.4 1.0 CZ C:PHE308 4.7 111.6 1.0 CB C:ALA390 4.9 115.6 1.0

Iron binding site 4 out of 4 in the Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Partial Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th). within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe500 b:148.5 occ:1.00 NE2 D:HIS330 2.2 115.2 1.0 NE2 D:HIS335 2.2 115.3 1.0 O D:HOH601 2.3 131.6 1.0 CD2 D:HIS335 2.4 115.3 1.0 CD2 D:HIS330 2.5 115.2 1.0 OE2 D:GLU375 2.7 118.3 1.0 CE1 D:HIS330 3.5 115.2 1.0 CE1 D:HIS335 3.5 115.3 1.0 CD D:GLU375 3.6 118.3 1.0 CG D:HIS335 3.7 115.3 1.0 OE1 D:GLU375 3.7 118.3 1.0 CG D:HIS330 3.8 115.2 1.0 CB D:PRO326 4.0 111.4 1.0 ND1 D:HIS335 4.2 115.3 1.0 ND1 D:HIS330 4.2 115.2 1.0 CZ D:PHE308 4.3 111.8 1.0 CB D:GLU331 4.5 121.7 1.0 OE1 D:GLU331 4.5 121.7 1.0 CE1 D:PHE308 4.7 111.8 1.0 CG D:PRO326 4.8 111.4 1.0 CB D:ALA390 4.8 116.7 1.0 CB D:HIS335 4.9 115.3 1.0 CG D:GLU375 5.0 118.3 1.0 CA D:GLU331 5.0 121.7 1.0

M.T.Bueno-Carrasco, J.Cuellar, M.I.Flydal, C.Santiago, T.A.Krakenes, R.Kleppe, J.R.Lopez-Blanco, K.Teigen, S.Alvira, P.Chacon, A.Martinez, J.M.Valpuesta. The Structure of Human Tyrosine Hydroxylase Reveals the Mechanism For Feedback Inhibition By Dopamine To Be Published.