Iron in PDB 7wiy: Cryo-Em Structure of Human TPH2 Tetramer
Enzymatic activity of Cryo-Em Structure of Human TPH2 Tetramer
All present enzymatic activity of Cryo-Em Structure of Human TPH2 Tetramer:
1.14.16.4;
Iron Binding Sites:
The binding sites of Iron atom in the Cryo-Em Structure of Human TPH2 Tetramer
(pdb code 7wiy). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Cryo-Em Structure of Human TPH2 Tetramer, PDB code: 7wiy:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 7wiy
Go back to
Iron Binding Sites List in 7wiy
Iron binding site 1 out
of 4 in the Cryo-Em Structure of Human TPH2 Tetramer
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Cryo-Em Structure of Human TPH2 Tetramer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe501
b:35.7
occ:1.00
|
NE2
|
B:HIS323
|
2.0
|
22.6
|
1.0
|
OE2
|
B:GLU363
|
2.1
|
27.3
|
1.0
|
NE2
|
B:HIS318
|
2.2
|
32.4
|
1.0
|
CD2
|
B:HIS323
|
2.8
|
22.6
|
1.0
|
CE1
|
B:HIS318
|
3.1
|
32.4
|
1.0
|
CE1
|
B:HIS323
|
3.1
|
22.6
|
1.0
|
CD
|
B:GLU363
|
3.2
|
27.3
|
1.0
|
CD2
|
B:HIS318
|
3.3
|
32.4
|
1.0
|
N3
|
B:IMD502
|
3.3
|
30.8
|
1.0
|
C2
|
B:IMD502
|
3.4
|
30.8
|
1.0
|
C4
|
B:IMD502
|
3.5
|
30.8
|
1.0
|
HN3
|
B:IMD502
|
3.6
|
30.8
|
1.0
|
N1
|
B:IMD502
|
3.7
|
30.8
|
1.0
|
C5
|
B:IMD502
|
3.7
|
30.8
|
1.0
|
OE1
|
B:GLU363
|
3.8
|
27.3
|
1.0
|
H2
|
B:IMD502
|
3.8
|
30.8
|
1.0
|
H4
|
B:IMD502
|
3.9
|
30.8
|
1.0
|
CG
|
B:HIS323
|
4.0
|
22.6
|
1.0
|
ND1
|
B:HIS323
|
4.1
|
22.6
|
1.0
|
HN1
|
B:IMD502
|
4.2
|
30.8
|
1.0
|
ND1
|
B:HIS318
|
4.2
|
32.4
|
1.0
|
H5
|
B:IMD502
|
4.2
|
30.8
|
1.0
|
CB
|
B:ALA378
|
4.2
|
28.0
|
1.0
|
CG
|
B:HIS318
|
4.4
|
32.4
|
1.0
|
CG
|
B:GLU363
|
4.4
|
27.3
|
1.0
|
OH
|
B:TYR358
|
4.9
|
26.1
|
1.0
|
|
Iron binding site 2 out
of 4 in 7wiy
Go back to
Iron Binding Sites List in 7wiy
Iron binding site 2 out
of 4 in the Cryo-Em Structure of Human TPH2 Tetramer
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Cryo-Em Structure of Human TPH2 Tetramer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe501
b:37.5
occ:1.00
|
HN3
|
C:IMD502
|
1.5
|
32.4
|
1.0
|
H2
|
C:IMD502
|
1.8
|
32.4
|
1.0
|
N3
|
C:IMD502
|
1.9
|
32.4
|
1.0
|
NE2
|
C:HIS323
|
1.9
|
23.6
|
1.0
|
NE2
|
C:HIS318
|
2.0
|
32.5
|
1.0
|
C2
|
C:IMD502
|
2.1
|
32.4
|
1.0
|
OE2
|
C:GLU363
|
2.4
|
28.1
|
1.0
|
CD2
|
C:HIS323
|
2.5
|
23.6
|
1.0
|
CE1
|
C:HIS318
|
2.8
|
32.5
|
1.0
|
CD2
|
C:HIS318
|
3.1
|
32.5
|
1.0
|
CE1
|
C:HIS323
|
3.1
|
23.6
|
1.0
|
C4
|
C:IMD502
|
3.3
|
32.4
|
1.0
|
N1
|
C:IMD502
|
3.4
|
32.4
|
1.0
|
CD
|
C:GLU363
|
3.5
|
28.1
|
1.0
|
CB
|
C:ALA378
|
3.7
|
27.4
|
1.0
|
CG
|
C:HIS323
|
3.8
|
23.6
|
1.0
|
H4
|
C:IMD502
|
3.9
|
32.4
|
1.0
|
OE1
|
C:GLU363
|
4.0
|
28.1
|
1.0
|
C5
|
C:IMD502
|
4.0
|
32.4
|
1.0
|
ND1
|
C:HIS318
|
4.0
|
32.5
|
1.0
|
ND1
|
C:HIS323
|
4.0
|
23.6
|
1.0
|
CG
|
C:HIS318
|
4.1
|
32.5
|
1.0
|
HN1
|
C:IMD502
|
4.1
|
32.4
|
1.0
|
CG
|
C:GLU363
|
4.7
|
28.1
|
1.0
|
O
|
C:HIS318
|
4.8
|
32.5
|
1.0
|
H5
|
C:IMD502
|
4.9
|
32.4
|
1.0
|
CG
|
C:GLU319
|
4.9
|
30.6
|
1.0
|
|
Iron binding site 3 out
of 4 in 7wiy
Go back to
Iron Binding Sites List in 7wiy
Iron binding site 3 out
of 4 in the Cryo-Em Structure of Human TPH2 Tetramer
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Cryo-Em Structure of Human TPH2 Tetramer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe501
b:35.7
occ:1.00
|
HN3
|
D:IMD502
|
1.5
|
31.7
|
1.0
|
H2
|
D:IMD502
|
1.8
|
31.7
|
1.0
|
NE2
|
D:HIS323
|
1.9
|
23.5
|
1.0
|
N3
|
D:IMD502
|
1.9
|
31.7
|
1.0
|
NE2
|
D:HIS318
|
2.0
|
32.7
|
1.0
|
C2
|
D:IMD502
|
2.1
|
31.7
|
1.0
|
OE2
|
D:GLU363
|
2.4
|
27.6
|
1.0
|
CD2
|
D:HIS323
|
2.5
|
23.5
|
1.0
|
CE1
|
D:HIS318
|
2.9
|
32.7
|
1.0
|
CD2
|
D:HIS318
|
3.0
|
32.7
|
1.0
|
CE1
|
D:HIS323
|
3.1
|
23.5
|
1.0
|
C4
|
D:IMD502
|
3.3
|
31.7
|
1.0
|
N1
|
D:IMD502
|
3.4
|
31.7
|
1.0
|
CD
|
D:GLU363
|
3.4
|
27.6
|
1.0
|
CG
|
D:HIS323
|
3.8
|
23.5
|
1.0
|
H4
|
D:IMD502
|
3.9
|
31.7
|
1.0
|
CB
|
D:ALA378
|
3.9
|
27.4
|
1.0
|
OE1
|
D:GLU363
|
3.9
|
27.6
|
1.0
|
C5
|
D:IMD502
|
4.0
|
31.7
|
1.0
|
ND1
|
D:HIS323
|
4.0
|
23.5
|
1.0
|
ND1
|
D:HIS318
|
4.0
|
32.7
|
1.0
|
CG
|
D:HIS318
|
4.1
|
32.7
|
1.0
|
HN1
|
D:IMD502
|
4.1
|
31.7
|
1.0
|
CG
|
D:GLU363
|
4.6
|
27.6
|
1.0
|
O
|
D:HIS318
|
4.8
|
32.7
|
1.0
|
CG
|
D:GLU319
|
4.8
|
31.1
|
1.0
|
H5
|
D:IMD502
|
4.9
|
31.7
|
1.0
|
|
Iron binding site 4 out
of 4 in 7wiy
Go back to
Iron Binding Sites List in 7wiy
Iron binding site 4 out
of 4 in the Cryo-Em Structure of Human TPH2 Tetramer
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Cryo-Em Structure of Human TPH2 Tetramer within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:37.1
occ:1.00
|
H5
|
A:IMD502
|
1.5
|
32.4
|
1.0
|
NE2
|
A:HIS323
|
1.9
|
23.0
|
1.0
|
OE2
|
A:GLU363
|
2.1
|
27.8
|
1.0
|
C5
|
A:IMD502
|
2.1
|
32.4
|
1.0
|
NE2
|
A:HIS318
|
2.1
|
32.8
|
1.0
|
CD2
|
A:HIS323
|
2.7
|
23.0
|
1.0
|
C4
|
A:IMD502
|
2.9
|
32.4
|
1.0
|
CE1
|
A:HIS318
|
2.9
|
32.8
|
1.0
|
N1
|
A:IMD502
|
3.0
|
32.4
|
1.0
|
CE1
|
A:HIS323
|
3.1
|
23.0
|
1.0
|
H4
|
A:IMD502
|
3.1
|
32.4
|
1.0
|
CD
|
A:GLU363
|
3.2
|
27.8
|
1.0
|
CD2
|
A:HIS318
|
3.2
|
32.8
|
1.0
|
HN1
|
A:IMD502
|
3.3
|
32.4
|
1.0
|
OE1
|
A:GLU363
|
3.8
|
27.8
|
1.0
|
N3
|
A:IMD502
|
3.9
|
32.4
|
1.0
|
CG
|
A:HIS323
|
4.0
|
23.0
|
1.0
|
C2
|
A:IMD502
|
4.0
|
32.4
|
1.0
|
ND1
|
A:HIS323
|
4.1
|
23.0
|
1.0
|
CB
|
A:ALA378
|
4.1
|
28.2
|
1.0
|
ND1
|
A:HIS318
|
4.1
|
32.8
|
1.0
|
CG
|
A:HIS318
|
4.3
|
32.8
|
1.0
|
CG
|
A:GLU363
|
4.4
|
27.8
|
1.0
|
HN3
|
A:IMD502
|
4.8
|
32.4
|
1.0
|
H2
|
A:IMD502
|
4.8
|
32.4
|
1.0
|
OH
|
A:TYR358
|
4.9
|
26.1
|
1.0
|
|
Reference:
K.Zhu,
C.Liu,
Y.Gao,
J.Lu,
D.Wang,
H.Zhang.
Cryo-Em Structure and Activator Screening of Human Tryptophan Hydroxylase 2. Front Pharmacol V. 13 07437 2022.
ISSN: ESSN 1663-9812
PubMed: 36046836
DOI: 10.3389/FPHAR.2022.907437
Page generated: Fri Aug 9 10:26:58 2024
|