Iron in PDB 7a2g: Full-Length Structure of the Substrate-Free Tyrosine Hydroxylase (Apo- Th).

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

The binding sites of Iron atom in the Full-Length Structure of the Substrate-Free Tyrosine Hydroxylase (Apo- Th). (pdb code 7a2g). 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 Structure of the Substrate-Free Tyrosine Hydroxylase (Apo- Th)., PDB code: 7a2g:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Full-Length 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 Full-Length Structure of the Substrate-Free Tyrosine Hydroxylase (Apo- Th). within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:287.2 occ:1.00 O A:HOH601 1.9 266.1 1.0 NE2 A:HIS335 1.9 263.9 1.0 NE2 A:HIS330 2.0 257.8 1.0 OE2 A:GLU375 2.6 254.8 1.0 CE1 A:HIS335 2.6 263.9 1.0 CD2 A:HIS335 2.8 263.9 1.0 CD2 A:HIS330 2.9 257.8 1.0 CE1 A:HIS330 3.1 257.8 1.0 OE1 A:GLU375 3.2 254.8 1.0 CD A:GLU375 3.2 254.8 1.0 ND1 A:HIS335 3.6 263.9 1.0 CG A:HIS335 3.7 263.9 1.0 CZ A:PHE308 3.8 286.4 1.0 OH A:TYR370 3.8 242.3 1.0 CG A:HIS330 4.1 257.8 1.0 ND1 A:HIS330 4.1 257.8 1.0 CE1 A:PHE308 4.4 286.4 1.0 CB A:PRO326 4.4 285.5 1.0 CG A:GLU375 4.7 254.8 1.0 CB A:GLU331 4.8 258.6 1.0 CE2 A:PHE308 4.8 286.4 1.0 CA A:GLU331 4.9 258.6 1.0

Iron binding site 2 out of 4 in the Full-Length 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 Full-Length Structure of the Substrate-Free Tyrosine Hydroxylase (Apo- Th). within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:290.7 occ:1.00 OE2 B:GLU375 1.9 266.1 1.0 O B:HOH601 1.9 268.8 1.0 NE2 B:HIS335 1.9 270.6 1.0 NE2 B:HIS330 1.9 264.8 1.0 OE1 B:GLU375 2.3 266.1 1.0 CD B:GLU375 2.4 266.1 1.0 CE1 B:HIS330 2.7 264.8 1.0 CE1 B:HIS335 2.7 270.6 1.0 CD2 B:HIS335 3.1 270.6 1.0 CD2 B:HIS330 3.1 264.8 1.0 OH B:TYR370 3.6 244.7 1.0 CG B:GLU375 3.8 266.1 1.0 ND1 B:HIS335 3.9 270.6 1.0 ND1 B:HIS330 3.9 264.8 1.0 CG B:HIS335 4.1 270.6 1.0 CG B:HIS330 4.1 264.8 1.0 CB B:PRO326 4.5 290.5 1.0 CZ B:PHE308 4.5 298.5 1.0 CB B:GLU375 4.7 266.1 1.0 CZ B:TYR370 4.8 244.7 1.0 CE1 B:PHE308 5.0 298.5 1.0 CB B:ALA390 5.0 269.4 1.0

Iron binding site 3 out of 4 in the Full-Length 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 Full-Length Structure of the Substrate-Free Tyrosine Hydroxylase (Apo- Th). within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:301.4 occ:1.00 O C:HOH601 1.9 274.7 1.0 OE2 C:GLU375 1.9 262.2 1.0 NE2 C:HIS330 1.9 262.4 1.0 NE2 C:HIS335 2.0 267.9 1.0 CE1 C:HIS330 2.2 262.4 1.0 CD C:GLU375 2.6 262.2 1.0 OE1 C:GLU375 2.7 262.2 1.0 CE1 C:HIS335 2.8 267.9 1.0 CD2 C:HIS335 3.0 267.9 1.0 CD2 C:HIS330 3.3 262.4 1.0 ND1 C:HIS330 3.5 262.4 1.0 OH C:TYR370 3.6 249.2 1.0 ND1 C:HIS335 3.9 267.9 1.0 CG C:GLU375 4.0 262.2 1.0 CG C:HIS335 4.0 267.9 1.0 CG C:HIS330 4.1 262.4 1.0 CZ C:PHE308 4.4 298.4 1.0 CB C:PRO326 4.6 291.9 1.0 CZ C:TYR370 4.8 249.2 1.0 CB C:ALA390 4.9 262.4 1.0

Iron binding site 4 out of 4 in the Full-Length 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 Full-Length Structure of the Substrate-Free Tyrosine Hydroxylase (Apo- Th). within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe501 b:310.3 occ:1.00 O D:HOH601 1.9 277.7 1.0 NE2 D:HIS335 1.9 279.4 1.0 NE2 D:HIS330 2.0 262.4 1.0 OE2 D:GLU375 2.0 266.7 1.0 CE1 D:HIS335 2.5 279.4 1.0 OE1 D:GLU375 2.7 266.7 1.0 CD D:GLU375 2.7 266.7 1.0 CD2 D:HIS330 2.7 262.4 1.0 OE2 D:GLU331 3.0 270.4 1.0 CD2 D:HIS335 3.0 279.4 1.0 CE1 D:HIS330 3.2 262.4 1.0 CG D:GLU331 3.6 270.4 1.0 ND1 D:HIS335 3.6 279.4 1.0 CD D:GLU331 3.7 270.4 1.0 OH D:TYR370 3.7 251.1 1.0 CG D:HIS335 3.9 279.4 1.0 CG D:HIS330 3.9 262.4 1.0 CG D:GLU375 4.1 266.7 1.0 ND1 D:HIS330 4.2 262.4 1.0 CB D:PRO326 4.2 286.1 1.0 CZ D:PHE308 4.4 294.0 1.0 CE1 D:PHE308 4.8 294.0 1.0 CB D:GLU331 4.8 270.4 1.0 OE1 D:GLU331 4.9 270.4 1.0 CG D:PRO326 4.9 286.1 1.0 CA D:GLU331 5.0 270.4 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. Full-Length Structure of the Substrate-Free Tyrosine Hydroxylase (Apo-Th). To Be Published.