Fluorine in PDB 7zik: Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401

Enzymatic activity of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401

All present enzymatic activity of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401:
1.14.16.4;

Protein crystallography data

The structure of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401, PDB code: 7zik was solved by A.Schuetz, U.Heinemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.01 / 2.59
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 47.09, 57.581, 62.587, 107.65, 93.14, 90.15
R / Rfree (%) 22.4 / 25.9

Other elements in 7zik:

The structure of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Iron (Fe) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401 (pdb code 7zik). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401, PDB code: 7zik:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 7zik

Go back to Fluorine Binding Sites List in 7zik
Fluorine binding site 1 out of 6 in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:65.4
occ:1.00
 F1 A:IVN502 0.0 65.4 1.0
CBL A:IVN502 1.3 60.1 1.0
F3 A:IVN502 2.2 65.0 1.0
F2 A:IVN502 2.2 54.6 1.0
CBJ A:IVN502 2.3 56.5 1.0
OAX A:IVN502 2.7 48.5 1.0
CB A:CYS364 3.3 44.2 1.0
CG2 A:ILE366 3.4 37.3 1.0
O A:CYS364 3.4 48.3 1.0
CE1 A:PHE313 3.5 37.4 1.0
CBG A:IVN502 3.6 59.4 1.0
C A:CYS364 3.6 44.8 1.0
C6 A:IVN502 3.6 47.4 1.0
CZ A:PHE313 3.8 40.0 1.0
O A:LEU365 3.9 43.2 1.0
C A:LEU365 4.1 43.4 1.0
CA A:CYS364 4.1 45.0 1.0
N A:LEU365 4.1 43.4 1.0
N1 A:IVN502 4.2 53.0 1.0
CD1 A:PHE313 4.2 37.6 1.0
CAP A:IVN502 4.4 58.0 1.0
CBH A:IVN502 4.4 57.5 1.0
NBK A:IVN502 4.4 59.3 1.0
C5 A:IVN502 4.5 45.8 1.0
N A:ILE366 4.5 44.0 1.0
CA A:LEU365 4.6 43.9 1.0
CAQ A:IVN502 4.6 59.1 1.0
CB A:ILE366 4.6 42.2 1.0
SG A:CYS364 4.7 26.0 1.0
CE2 A:PHE313 4.7 44.2 1.0
NAW A:IVN502 4.8 62.0 1.0
CA A:ILE366 4.9 44.5 1.0

Fluorine binding site 2 out of 6 in 7zik

Go back to Fluorine Binding Sites List in 7zik
Fluorine binding site 2 out of 6 in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:65.0
occ:1.00
 F3 A:IVN502 0.0 65.0 1.0
CBL A:IVN502 1.3 60.1 1.0
F1 A:IVN502 2.2 65.4 1.0
F2 A:IVN502 2.2 54.6 1.0
CBJ A:IVN502 2.3 56.5 1.0
CBG A:IVN502 2.7 59.4 1.0
OAX A:IVN502 2.8 48.5 1.0
CAP A:IVN502 3.1 58.0 1.0
CG2 A:ILE366 3.1 37.3 1.0
CBH A:IVN502 3.6 57.5 1.0
NBK A:IVN502 4.1 59.3 1.0
C6 A:IVN502 4.2 47.4 1.0
CAJ A:IVN502 4.2 52.7 1.0
O A:CYS364 4.2 48.3 1.0
CB A:ILE366 4.4 42.2 1.0
NAW A:IVN502 4.4 62.0 1.0
CG1 A:ILE366 4.5 41.9 1.0
CD1 A:ILE366 4.5 41.1 1.0
CAR A:IVN502 4.5 54.6 1.0
CBB A:IVN502 4.8 52.8 1.0
N1 A:IVN502 4.8 53.0 1.0
CB A:CYS364 4.9 44.2 1.0
CAQ A:IVN502 4.9 59.1 1.0
C A:CYS364 4.9 44.8 1.0

Fluorine binding site 3 out of 6 in 7zik

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Fluorine binding site 3 out of 6 in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:54.6
occ:1.00
 F2 A:IVN502 0.0 54.6 1.0
CBL A:IVN502 1.3 60.1 1.0
F3 A:IVN502 2.2 65.0 1.0
F1 A:IVN502 2.2 65.4 1.0
CBJ A:IVN502 2.4 56.5 1.0
NBK A:IVN502 2.7 59.3 1.0
NAW A:IVN502 2.8 62.0 1.0
CBG A:IVN502 2.9 59.4 1.0
CBH A:IVN502 3.0 57.5 1.0
CAQ A:IVN502 3.3 59.1 1.0
CAZ A:IVN502 3.3 61.7 1.0
CB A:CYS364 3.5 44.2 1.0
OAX A:IVN502 3.6 48.5 1.0
CAK A:IVN502 3.7 59.2 1.0
CAP A:IVN502 4.0 58.0 1.0
O A:CYS364 4.1 48.3 1.0
CAR A:IVN502 4.2 54.6 1.0
CAA A:IVN502 4.3 61.1 1.0
SG A:CYS364 4.4 26.0 1.0
C6 A:IVN502 4.6 47.4 1.0
C A:CYS364 4.6 44.8 1.0
CA A:CYS364 4.6 45.0 1.0
N1 A:IVN502 4.7 53.0 1.0
CE1 A:PHE313 4.8 37.4 1.0
CD1 A:PHE313 4.9 37.6 1.0
CG2 A:ILE366 4.9 37.3 1.0
CAJ A:IVN502 5.0 52.7 1.0

Fluorine binding site 4 out of 6 in 7zik

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Fluorine binding site 4 out of 6 in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F502

b:70.8
occ:1.00
 F1 B:IVN502 0.0 70.8 1.0
CBL B:IVN502 1.3 73.2 1.0
F3 B:IVN502 2.2 76.2 1.0
F2 B:IVN502 2.2 77.7 1.0
CBJ B:IVN502 2.4 67.7 1.0
NAW B:IVN502 2.6 67.9 1.0
CBG B:IVN502 2.8 67.6 1.0
NBK B:IVN502 2.9 65.6 1.0
CBH B:IVN502 3.0 63.1 1.0
CAZ B:IVN502 3.6 66.9 1.0
OAX B:IVN502 3.6 60.3 1.0
CB B:CYS364 3.7 44.1 1.0
CAP B:IVN502 3.8 65.9 1.0
CAQ B:IVN502 4.0 67.2 1.0
CAR B:IVN502 4.1 57.8 1.0
O B:HOH628 4.2 41.1 1.0
O B:CYS364 4.3 46.5 1.0
CAA B:IVN502 4.3 63.2 1.0
CAK B:IVN502 4.4 69.0 1.0
C6 B:IVN502 4.6 50.4 1.0
N1 B:IVN502 4.7 46.0 1.0
C B:CYS364 4.7 46.2 1.0
SG B:CYS364 4.8 52.5 1.0
CAJ B:IVN502 4.8 59.0 1.0
CA B:CYS364 4.9 47.0 1.0
CBB B:IVN502 4.9 57.5 1.0

Fluorine binding site 5 out of 6 in 7zik

Go back to Fluorine Binding Sites List in 7zik
Fluorine binding site 5 out of 6 in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F502

b:76.2
occ:1.00
 F3 B:IVN502 0.0 76.2 1.0
CBL B:IVN502 1.3 73.2 1.0
F1 B:IVN502 2.2 70.8 1.0
F2 B:IVN502 2.2 77.7 1.0
CBJ B:IVN502 2.4 67.7 1.0
OAX B:IVN502 2.8 60.3 1.0
CB B:CYS364 3.3 44.1 1.0
O B:CYS364 3.5 46.5 1.0
CBG B:IVN502 3.6 67.6 1.0
CE1 B:PHE313 3.6 32.8 1.0
C B:CYS364 3.7 46.2 1.0
C6 B:IVN502 3.7 50.4 1.0
O B:LEU365 3.7 54.0 1.0
NAW B:IVN502 3.9 67.9 1.0
CZ B:PHE313 3.9 36.2 1.0
C B:LEU365 4.0 55.0 1.0
CA B:CYS364 4.1 47.0 1.0
N B:LEU365 4.1 49.2 1.0
N1 B:IVN502 4.2 46.0 1.0
CD1 B:PHE313 4.3 30.5 1.0
CAP B:IVN502 4.4 65.9 1.0
CBH B:IVN502 4.4 63.1 1.0
N B:ILE366 4.4 57.6 1.0
NBK B:IVN502 4.5 65.6 1.0
C5 B:IVN502 4.5 45.9 1.0
CB B:ILE366 4.5 72.3 1.0
CA B:LEU365 4.6 53.4 1.0
SG B:CYS364 4.8 52.5 1.0
CA B:ILE366 4.8 58.7 1.0
CE2 B:PHE313 4.8 37.0 1.0
CAZ B:IVN502 4.9 66.9 1.0

Fluorine binding site 6 out of 6 in 7zik

Go back to Fluorine Binding Sites List in 7zik
Fluorine binding site 6 out of 6 in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor LP533401 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:F502

b:77.7
occ:1.00
 F2 B:IVN502 0.0 77.7 1.0
CBL B:IVN502 1.4 73.2 1.0
F3 B:IVN502 2.2 76.2 1.0
F1 B:IVN502 2.2 70.8 1.0
CBJ B:IVN502 2.4 67.7 1.0
OAX B:IVN502 2.8 60.3 1.0
CBG B:IVN502 2.8 67.6 1.0
CAP B:IVN502 3.1 65.9 1.0
CB B:ILE366 3.8 72.3 1.0
CBH B:IVN502 3.8 63.1 1.0
C6 B:IVN502 4.1 50.4 1.0
CAJ B:IVN502 4.2 59.0 1.0
CD1 B:ILE366 4.2 69.7 1.0
O B:CYS364 4.3 46.5 1.0
CG1 B:ILE366 4.3 71.7 1.0
CG2 B:ILE366 4.4 73.0 1.0
NAW B:IVN502 4.4 67.9 1.0
NBK B:IVN502 4.4 65.6 1.0
N B:ILE366 4.6 57.6 1.0
CA B:ILE366 4.7 58.7 1.0
CAR B:IVN502 4.8 57.8 1.0
C B:LEU365 4.8 55.0 1.0
N1 B:IVN502 4.8 46.0 1.0
O B:LEU365 4.9 54.0 1.0
CBB B:IVN502 4.9 57.5 1.0
C B:CYS364 5.0 46.2 1.0

Reference:

E.Specker, S.Matthes, R.Wesolowski, A.Schutz, M.Grohmann, N.Alenina, D.Pleimes, K.Mallow, M.Neuenschwander, A.Gogolin, M.Weise, J.Pfeifer, N.Ziebart, U.Heinemann, J.P.Von Kries, M.Nazare, M.Bader. Structure-Based Design of Xanthine-Benzimidazole Derivatives As Novel and Potent Tryptophan Hydroxylase Inhibitors. J.Med.Chem. V. 65 11126 2022.
ISSN: ISSN 0022-2623
PubMed: 35921615
DOI: 10.1021/ACS.JMEDCHEM.2C00598
Page generated: Fri Aug 2 16:09:36 2024

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