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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

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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: Thu Aug 7 09:52:19 2025

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