Iron in PDB 6zvp: Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms
Enzymatic activity of Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms
All present enzymatic activity of Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms:
1.14.16.2;
Iron Binding Sites:
The binding sites of Iron atom in the Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms
(pdb code 6zvp). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms, PDB code: 6zvp:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 6zvp
Go back to
Iron Binding Sites List in 6zvp
Iron binding site 1 out
of 4 in the Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe501
b:205.4
occ:1.00
|
CE1
|
D:HIS330
|
1.7
|
292.2
|
1.0
|
OE2
|
D:GLU375
|
2.0
|
175.1
|
1.0
|
O1
|
D:LDP502
|
2.0
|
315.7
|
1.0
|
OE1
|
D:GLU375
|
2.0
|
229.5
|
1.0
|
NE2
|
D:HIS335
|
2.1
|
192.1
|
1.0
|
NE2
|
D:HIS330
|
2.2
|
246.0
|
1.0
|
O2
|
D:LDP502
|
2.3
|
132.6
|
1.0
|
CD
|
D:GLU375
|
2.3
|
208.8
|
1.0
|
CE1
|
D:HIS335
|
2.6
|
305.1
|
1.0
|
C3
|
D:LDP502
|
2.9
|
233.2
|
1.0
|
C4
|
D:LDP502
|
3.0
|
198.9
|
1.0
|
ND1
|
D:HIS330
|
3.0
|
283.4
|
1.0
|
CD2
|
D:HIS335
|
3.1
|
159.4
|
1.0
|
CB
|
D:ALA390
|
3.1
|
359.4
|
1.0
|
CD2
|
D:HIS330
|
3.5
|
143.6
|
1.0
|
ND1
|
D:HIS335
|
3.7
|
320.3
|
1.0
|
CG
|
D:GLU375
|
3.8
|
187.5
|
1.0
|
CG
|
D:HIS330
|
3.9
|
209.7
|
1.0
|
CG
|
D:HIS335
|
3.9
|
224.6
|
1.0
|
N
|
D:GLY391
|
4.0
|
181.0
|
1.0
|
C
|
D:ALA390
|
4.1
|
183.8
|
1.0
|
C2
|
D:LDP502
|
4.2
|
224.0
|
1.0
|
CA
|
D:ALA390
|
4.2
|
296.2
|
1.0
|
C5
|
D:LDP502
|
4.3
|
259.6
|
1.0
|
O
|
D:ALA390
|
4.6
|
125.1
|
1.0
|
CB
|
D:GLU375
|
4.6
|
205.4
|
1.0
|
CA
|
D:GLY391
|
4.7
|
174.2
|
1.0
|
CA
|
D:GLU375
|
4.7
|
254.1
|
1.0
|
OH
|
D:TYR370
|
4.7
|
229.2
|
1.0
|
|
Iron binding site 2 out
of 4 in 6zvp
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Iron Binding Sites List in 6zvp
Iron binding site 2 out
of 4 in the Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:205.4
occ:1.00
|
CE1
|
A:HIS330
|
1.7
|
292.2
|
1.0
|
OE2
|
A:GLU375
|
2.0
|
175.1
|
1.0
|
O1
|
A:LDP502
|
2.0
|
315.7
|
1.0
|
OE1
|
A:GLU375
|
2.0
|
229.5
|
1.0
|
NE2
|
A:HIS335
|
2.1
|
192.1
|
1.0
|
NE2
|
A:HIS330
|
2.2
|
246.0
|
1.0
|
O2
|
A:LDP502
|
2.3
|
132.6
|
1.0
|
CD
|
A:GLU375
|
2.3
|
208.8
|
1.0
|
CE1
|
A:HIS335
|
2.6
|
305.1
|
1.0
|
C3
|
A:LDP502
|
2.9
|
233.2
|
1.0
|
C4
|
A:LDP502
|
3.0
|
198.9
|
1.0
|
ND1
|
A:HIS330
|
3.0
|
283.4
|
1.0
|
CD2
|
A:HIS335
|
3.1
|
159.4
|
1.0
|
CB
|
A:ALA390
|
3.1
|
359.4
|
1.0
|
CD2
|
A:HIS330
|
3.5
|
143.6
|
1.0
|
ND1
|
A:HIS335
|
3.7
|
320.3
|
1.0
|
CG
|
A:GLU375
|
3.8
|
187.5
|
1.0
|
CG
|
A:HIS330
|
3.9
|
209.7
|
1.0
|
CG
|
A:HIS335
|
3.9
|
224.6
|
1.0
|
N
|
A:GLY391
|
4.0
|
181.0
|
1.0
|
C
|
A:ALA390
|
4.1
|
183.8
|
1.0
|
C2
|
A:LDP502
|
4.2
|
224.0
|
1.0
|
CA
|
A:ALA390
|
4.2
|
296.2
|
1.0
|
C5
|
A:LDP502
|
4.3
|
259.6
|
1.0
|
O
|
A:ALA390
|
4.6
|
125.1
|
1.0
|
CB
|
A:GLU375
|
4.6
|
205.4
|
1.0
|
CA
|
A:GLY391
|
4.7
|
174.2
|
1.0
|
CA
|
A:GLU375
|
4.7
|
254.1
|
1.0
|
OH
|
A:TYR370
|
4.8
|
229.2
|
1.0
|
|
Iron binding site 3 out
of 4 in 6zvp
Go back to
Iron Binding Sites List in 6zvp
Iron binding site 3 out
of 4 in the Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe501
b:205.4
occ:1.00
|
CE1
|
B:HIS330
|
1.7
|
292.2
|
1.0
|
OE2
|
B:GLU375
|
2.0
|
175.1
|
1.0
|
O1
|
B:LDP502
|
2.0
|
315.7
|
1.0
|
OE1
|
B:GLU375
|
2.0
|
229.5
|
1.0
|
NE2
|
B:HIS335
|
2.1
|
192.1
|
1.0
|
NE2
|
B:HIS330
|
2.2
|
246.0
|
1.0
|
O2
|
B:LDP502
|
2.3
|
132.6
|
1.0
|
CD
|
B:GLU375
|
2.3
|
208.8
|
1.0
|
CE1
|
B:HIS335
|
2.6
|
305.1
|
1.0
|
C3
|
B:LDP502
|
2.9
|
233.2
|
1.0
|
C4
|
B:LDP502
|
3.0
|
198.9
|
1.0
|
ND1
|
B:HIS330
|
3.0
|
283.4
|
1.0
|
CD2
|
B:HIS335
|
3.1
|
159.4
|
1.0
|
CB
|
B:ALA390
|
3.1
|
359.4
|
1.0
|
CD2
|
B:HIS330
|
3.5
|
143.6
|
1.0
|
ND1
|
B:HIS335
|
3.7
|
320.3
|
1.0
|
CG
|
B:GLU375
|
3.8
|
187.5
|
1.0
|
CG
|
B:HIS330
|
3.9
|
209.7
|
1.0
|
CG
|
B:HIS335
|
3.9
|
224.6
|
1.0
|
N
|
B:GLY391
|
4.0
|
181.0
|
1.0
|
C
|
B:ALA390
|
4.1
|
183.8
|
1.0
|
C2
|
B:LDP502
|
4.2
|
224.0
|
1.0
|
CA
|
B:ALA390
|
4.2
|
296.2
|
1.0
|
C5
|
B:LDP502
|
4.3
|
259.6
|
1.0
|
O
|
B:ALA390
|
4.6
|
125.1
|
1.0
|
CB
|
B:GLU375
|
4.6
|
205.4
|
1.0
|
CA
|
B:GLY391
|
4.7
|
174.2
|
1.0
|
CA
|
B:GLU375
|
4.7
|
254.1
|
1.0
|
OH
|
B:TYR370
|
4.7
|
229.2
|
1.0
|
|
Iron binding site 4 out
of 4 in 6zvp
Go back to
Iron Binding Sites List in 6zvp
Iron binding site 4 out
of 4 in the Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Atomic Model of the Em-Based Structure of the Full-Length Tyrosine Hydroxylase in Complex with Dopamine (Residues 40-497) in Which the Regulatory Domain (Residues 40-165) Has Been Included Only with the Backbone Atoms within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe501
b:205.4
occ:1.00
|
CE1
|
C:HIS330
|
1.7
|
292.2
|
1.0
|
OE2
|
C:GLU375
|
2.0
|
175.1
|
1.0
|
O1
|
C:LDP502
|
2.0
|
315.7
|
1.0
|
OE1
|
C:GLU375
|
2.0
|
229.5
|
1.0
|
NE2
|
C:HIS335
|
2.1
|
192.1
|
1.0
|
NE2
|
C:HIS330
|
2.2
|
246.0
|
1.0
|
O2
|
C:LDP502
|
2.3
|
132.6
|
1.0
|
CD
|
C:GLU375
|
2.3
|
208.8
|
1.0
|
CE1
|
C:HIS335
|
2.6
|
305.1
|
1.0
|
C3
|
C:LDP502
|
2.9
|
233.2
|
1.0
|
C4
|
C:LDP502
|
3.0
|
198.9
|
1.0
|
ND1
|
C:HIS330
|
3.0
|
283.4
|
1.0
|
CD2
|
C:HIS335
|
3.1
|
159.4
|
1.0
|
CB
|
C:ALA390
|
3.1
|
359.4
|
1.0
|
CD2
|
C:HIS330
|
3.5
|
143.6
|
1.0
|
ND1
|
C:HIS335
|
3.7
|
320.3
|
1.0
|
CG
|
C:GLU375
|
3.8
|
187.5
|
1.0
|
CG
|
C:HIS330
|
3.9
|
209.7
|
1.0
|
CG
|
C:HIS335
|
3.9
|
224.6
|
1.0
|
N
|
C:GLY391
|
4.0
|
181.0
|
1.0
|
C
|
C:ALA390
|
4.1
|
183.8
|
1.0
|
C2
|
C:LDP502
|
4.2
|
224.0
|
1.0
|
CA
|
C:ALA390
|
4.2
|
296.2
|
1.0
|
C5
|
C:LDP502
|
4.3
|
259.6
|
1.0
|
O
|
C:ALA390
|
4.6
|
125.1
|
1.0
|
CB
|
C:GLU375
|
4.6
|
205.4
|
1.0
|
CA
|
C:GLY391
|
4.7
|
174.2
|
1.0
|
CA
|
C:GLU375
|
4.7
|
254.1
|
1.0
|
OH
|
C:TYR370
|
4.8
|
229.2
|
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 21:09:33 2024
|