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Iron in PDB 6zn2: Partial Structure of Tyrosine Hydroxylase in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding.

Enzymatic activity of Partial Structure of Tyrosine Hydroxylase in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding.

All present enzymatic activity of Partial Structure of Tyrosine Hydroxylase in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding.:
1.14.16.2;

Iron Binding Sites:

The binding sites of Iron atom in the Partial Structure of Tyrosine Hydroxylase in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding. (pdb code 6zn2). 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 in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding., PDB code: 6zn2:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 6zn2

Go back to Iron Binding Sites List in 6zn2
Iron binding site 1 out of 4 in the Partial Structure of Tyrosine Hydroxylase in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding.


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 in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:205.4
occ:1.00
O2 A:LDP501 2.1 132.6 1.0
O1 A:LDP501 2.1 315.7 1.0
NE2 A:HIS330 2.1 246.0 1.0
NE2 A:HIS335 2.2 192.1 1.0
OE2 A:GLU375 2.5 229.5 1.0
OE1 A:GLU375 2.6 175.1 1.0
C4 A:LDP501 2.8 198.9 1.0
C3 A:LDP501 2.8 233.2 1.0
CD A:GLU375 2.9 208.8 1.0
CD2 A:HIS330 2.9 143.6 1.0
CE1 A:HIS335 3.1 305.1 1.0
CD2 A:HIS335 3.1 159.4 1.0
CE1 A:HIS330 3.3 292.2 1.0
CG A:HIS330 4.1 209.7 1.0
C5 A:LDP501 4.2 259.6 1.0
C2 A:LDP501 4.2 224.0 1.0
CB A:PRO326 4.2 288.4 1.0
ND1 A:HIS335 4.2 320.3 1.0
ND1 A:HIS330 4.3 283.4 1.0
CG A:HIS335 4.3 224.6 1.0
CG A:GLU375 4.3 187.5 1.0
CB A:ALA390 4.5 359.4 1.0
OH A:TYR370 4.6 229.2 1.0
CG A:PRO326 4.7 297.3 1.0

Iron binding site 2 out of 4 in 6zn2

Go back to Iron Binding Sites List in 6zn2
Iron binding site 2 out of 4 in the Partial Structure of Tyrosine Hydroxylase in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding.


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 in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe502

b:205.4
occ:1.00
O2 C:LDP501 2.1 132.6 1.0
O1 C:LDP501 2.1 315.7 1.0
NE2 C:HIS330 2.1 246.0 1.0
NE2 C:HIS335 2.2 192.1 1.0
OE2 C:GLU375 2.5 229.5 1.0
OE1 C:GLU375 2.6 175.1 1.0
C4 C:LDP501 2.8 198.9 1.0
C3 C:LDP501 2.8 233.2 1.0
CD C:GLU375 2.9 208.8 1.0
CD2 C:HIS330 2.9 143.6 1.0
CE1 C:HIS335 3.1 305.1 1.0
CD2 C:HIS335 3.1 159.4 1.0
CE1 C:HIS330 3.3 292.2 1.0
CG C:HIS330 4.1 209.7 1.0
C5 C:LDP501 4.2 259.6 1.0
C2 C:LDP501 4.2 224.0 1.0
CB C:PRO326 4.2 288.4 1.0
ND1 C:HIS335 4.2 320.3 1.0
ND1 C:HIS330 4.3 283.4 1.0
CG C:HIS335 4.3 224.6 1.0
CG C:GLU375 4.3 187.5 1.0
CB C:ALA390 4.5 359.4 1.0
OH C:TYR370 4.6 229.2 1.0
CG C:PRO326 4.7 297.3 1.0

Iron binding site 3 out of 4 in 6zn2

Go back to Iron Binding Sites List in 6zn2
Iron binding site 3 out of 4 in the Partial Structure of Tyrosine Hydroxylase in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding.


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 in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe502

b:205.4
occ:1.00
O2 E:LDP501 2.1 132.6 1.0
O1 E:LDP501 2.1 315.7 1.0
NE2 E:HIS330 2.1 246.0 1.0
NE2 E:HIS335 2.2 192.1 1.0
OE2 E:GLU375 2.5 229.5 1.0
OE1 E:GLU375 2.6 175.1 1.0
C4 E:LDP501 2.8 198.9 1.0
C3 E:LDP501 2.8 233.2 1.0
CD E:GLU375 2.9 208.8 1.0
CD2 E:HIS330 2.9 143.6 1.0
CE1 E:HIS335 3.1 305.1 1.0
CD2 E:HIS335 3.1 159.4 1.0
CE1 E:HIS330 3.3 292.2 1.0
CG E:HIS330 4.1 209.7 1.0
C5 E:LDP501 4.2 259.6 1.0
C2 E:LDP501 4.2 224.0 1.0
CB E:PRO326 4.2 288.4 1.0
ND1 E:HIS335 4.2 320.3 1.0
ND1 E:HIS330 4.3 283.4 1.0
CG E:HIS335 4.3 224.6 1.0
CG E:GLU375 4.3 187.5 1.0
CB E:ALA390 4.5 359.4 1.0
OH E:TYR370 4.6 229.2 1.0
CG E:PRO326 4.7 297.3 1.0

Iron binding site 4 out of 4 in 6zn2

Go back to Iron Binding Sites List in 6zn2
Iron binding site 4 out of 4 in the Partial Structure of Tyrosine Hydroxylase in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding.


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 in Complex with Dopamine Showing the Catalytic Domain and An Alpha-Helix From the Regulatory Domain Involved in Dopamine Binding. within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe502

b:205.4
occ:1.00
O2 G:LDP501 2.1 132.6 1.0
O1 G:LDP501 2.1 315.7 1.0
NE2 G:HIS330 2.1 246.0 1.0
NE2 G:HIS335 2.2 192.1 1.0
OE2 G:GLU375 2.5 229.5 1.0
OE1 G:GLU375 2.6 175.1 1.0
C4 G:LDP501 2.8 198.9 1.0
C3 G:LDP501 2.8 233.2 1.0
CD G:GLU375 2.9 208.8 1.0
CD2 G:HIS330 2.9 143.6 1.0
CE1 G:HIS335 3.1 305.1 1.0
CD2 G:HIS335 3.1 159.4 1.0
CE1 G:HIS330 3.3 292.2 1.0
CG G:HIS330 4.1 209.7 1.0
C5 G:LDP501 4.2 259.6 1.0
C2 G:LDP501 4.2 224.0 1.0
CB G:PRO326 4.2 288.4 1.0
ND1 G:HIS335 4.2 320.3 1.0
ND1 G:HIS330 4.3 283.4 1.0
CG G:HIS335 4.3 224.6 1.0
CG G:GLU375 4.3 187.5 1.0
CB G:ALA390 4.5 359.4 1.0
OH G:TYR370 4.6 229.2 1.0
CG G:PRO326 4.7 297.3 1.0

Reference:

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.
Page generated: Wed Aug 7 20:39:17 2024

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