Iron in PDB 7pim: Partial Structure of Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine.

All present enzymatic activity of Partial Structure of Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine.:
1.14.16.2;

The binding sites of Iron atom in the Partial Structure of Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine. (pdb code 7pim). 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 Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine., PDB code: 7pim:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Partial Structure of Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine.


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 Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:331.1 occ:1.00 OE2 B:GLU375 2.0 266.8 1.0 O1 B:LDP501 2.0 276.0 1.0 O2 B:LDP501 2.1 276.0 1.0 NE2 B:HIS335 2.1 237.1 1.0 NE2 B:HIS330 2.2 264.4 1.0 C3 B:LDP501 2.6 276.0 1.0 C4 B:LDP501 2.6 276.0 1.0 CD B:GLU375 2.7 266.8 1.0 OE1 B:GLU375 2.7 266.8 1.0 CE1 B:HIS335 2.8 237.1 1.0 CE1 B:HIS330 3.1 264.4 1.0 CD2 B:HIS330 3.1 264.4 1.0 CD2 B:HIS335 3.3 237.1 1.0 C2 B:LDP501 3.8 276.0 1.0 C5 B:LDP501 3.9 276.0 1.0 ND1 B:HIS335 4.0 237.1 1.0 CG B:GLU375 4.1 266.8 1.0 ND1 B:HIS330 4.1 264.4 1.0 CG B:HIS330 4.2 264.4 1.0 CG B:HIS335 4.3 237.1 1.0 OH B:TYR370 4.5 236.9 1.0 CB B:ALA390 4.5 240.1 1.0 C1 B:LDP501 4.8 276.0 1.0 C6 B:LDP501 4.8 276.0 1.0 CB B:PRO326 4.9 296.3 1.0

Iron binding site 2 out of 4 in the Partial Structure of Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine.


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 Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:331.7 occ:1.00 OE2 A:GLU375 2.0 268.6 1.0 O1 A:LDP501 2.0 275.6 1.0 O2 A:LDP501 2.1 275.6 1.0 NE2 A:HIS335 2.1 235.2 1.0 NE2 A:HIS330 2.2 267.1 1.0 C3 A:LDP501 2.6 275.6 1.0 C4 A:LDP501 2.6 275.6 1.0 CD A:GLU375 2.7 268.6 1.0 OE1 A:GLU375 2.7 268.6 1.0 CE1 A:HIS335 2.8 235.2 1.0 CE1 A:HIS330 3.1 267.1 1.0 CD2 A:HIS330 3.1 267.1 1.0 CD2 A:HIS335 3.3 235.2 1.0 C2 A:LDP501 3.8 275.6 1.0 C5 A:LDP501 3.9 275.6 1.0 ND1 A:HIS335 4.0 235.2 1.0 CG A:GLU375 4.1 268.6 1.0 ND1 A:HIS330 4.1 267.1 1.0 CG A:HIS330 4.2 267.1 1.0 CG A:HIS335 4.3 235.2 1.0 OH A:TYR370 4.5 240.8 1.0 CB A:ALA390 4.5 241.0 1.0 C1 A:LDP501 4.8 275.6 1.0 C6 A:LDP501 4.8 275.6 1.0 CB A:PRO326 4.9 295.9 1.0

Iron binding site 3 out of 4 in the Partial Structure of Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine.


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 Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine. within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe502 b:327.4 occ:1.00 OE2 D:GLU375 2.0 264.8 1.0 O1 D:LDP501 2.0 275.8 1.0 O2 D:LDP501 2.1 275.8 1.0 NE2 D:HIS335 2.1 238.6 1.0 NE2 D:HIS330 2.2 263.9 1.0 C3 D:LDP501 2.6 275.8 1.0 C4 D:LDP501 2.6 275.8 1.0 CD D:GLU375 2.7 264.8 1.0 OE1 D:GLU375 2.7 264.8 1.0 CE1 D:HIS335 2.8 238.6 1.0 CE1 D:HIS330 3.1 263.9 1.0 CD2 D:HIS330 3.1 263.9 1.0 CD2 D:HIS335 3.3 238.6 1.0 C2 D:LDP501 3.8 275.8 1.0 C5 D:LDP501 3.9 275.8 1.0 ND1 D:HIS335 4.0 238.6 1.0 CG D:GLU375 4.1 264.8 1.0 ND1 D:HIS330 4.1 263.9 1.0 CG D:HIS330 4.2 263.9 1.0 CG D:HIS335 4.3 238.6 1.0 OH D:TYR370 4.5 238.2 1.0 CB D:ALA390 4.5 243.9 1.0 C1 D:LDP501 4.8 275.8 1.0 C6 D:LDP501 4.8 275.8 1.0 CB D:PRO326 4.9 298.7 1.0

Iron binding site 4 out of 4 in the Partial Structure of Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine.


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 Tyrosine Hydroxylase Lacking the First 35 Residues in Complex with Dopamine. within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe502 b:329.9 occ:1.00 OE2 F:GLU375 2.0 267.7 1.0 O1 F:LDP501 2.0 274.4 1.0 O2 F:LDP501 2.1 274.4 1.0 NE2 F:HIS335 2.1 236.2 1.0 NE2 F:HIS330 2.2 260.6 1.0 C3 F:LDP501 2.6 274.4 1.0 C4 F:LDP501 2.6 274.4 1.0 CD F:GLU375 2.7 267.7 1.0 OE1 F:GLU375 2.7 267.7 1.0 CE1 F:HIS335 2.8 236.2 1.0 CE1 F:HIS330 3.1 260.6 1.0 CD2 F:HIS330 3.1 260.6 1.0 CD2 F:HIS335 3.3 236.2 1.0 C2 F:LDP501 3.8 274.4 1.0 C5 F:LDP501 3.9 274.4 1.0 ND1 F:HIS335 4.0 236.2 1.0 CG F:GLU375 4.1 267.7 1.0 ND1 F:HIS330 4.1 260.6 1.0 CG F:HIS330 4.2 260.6 1.0 CG F:HIS335 4.3 236.2 1.0 OH F:TYR370 4.5 234.7 1.0 CB F:ALA390 4.5 245.1 1.0 C1 F:LDP501 4.8 274.4 1.0 C6 F:LDP501 4.8 274.4 1.0 CB F:PRO326 4.9 297.0 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. Structural Mechanism For Tyrosine Hydroxylase Inhibition By Dopamine and Reactivation By SER40 Phosphorylation To Be Published.