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
|