Chlorine in PDB 8cjo: Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004

Enzymatic activity of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004

All present enzymatic activity of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004:
1.14.16.4;

Protein crystallography data

The structure of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004, PDB code: 8cjo was solved by A.Schuetz, K.Mallow, M.Nazare, E.Specker, U.Heinemann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.31 / 1.87
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.218, 57.776, 69.6, 90, 109.35, 90
R / Rfree (%) 16.9 / 20.9

Other elements in 8cjo:

The structure of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004 also contains other interesting chemical elements:

Fluorine (F) 1 atom
Iron (Fe) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004 (pdb code 8cjo). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004, PDB code: 8cjo:

Chlorine binding site 1 out of 1 in 8cjo

Go back to Chlorine Binding Sites List in 8cjo
Chlorine binding site 1 out of 1 in the Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Tryptophan Hydroxylase 1 in Complex with Inhibitor Km-06-004 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:87.8
occ:1.00
 CLA A:UWL502 0.0 87.8 1.0
CAX A:UWL502 1.8 37.8 1.0
CAJ A:UWL502 2.8 29.7 1.0
CAG A:UWL502 2.8 34.8 1.0
CAB A:UWL502 3.8 34.3 1.0
O A:HOH873 3.8 46.0 1.0
CG1 A:ILE366 3.9 41.7 1.0
CB A:CYS364 3.9 28.5 1.0
CAY A:UWL502 4.0 31.4 1.0
CAI A:UWL502 4.1 38.7 1.0
CD1 A:ILE366 4.1 33.8 1.0
O A:CYS364 4.2 37.9 1.0
CAW A:UWL502 4.4 28.5 1.0
CBD A:UWL502 4.6 32.6 1.0
CE1 A:PHE313 4.6 26.0 1.0
O A:HOH676 4.7 32.5 1.0
C A:CYS364 4.8 34.8 1.0
CD1 A:PHE313 4.9 23.7 1.0
CAF A:UWL502 4.9 29.2 1.0

Reference:

E.Specker, R.Wesolowski, A.Schutz, S.Matthes, K.Mallow, M.Wasinska-Kalwa, L.Winkler, A.Oder, N.Alenina, D.Pleimes, J.P.Von Kries, U.Heinemann, M.Bader, M.Nazare. Structure-Based Design of Xanthine-Imidazopyridines and -Imidazothiazoles As Highly Potent and in Vivo Efficacious Tryptophan Hydroxylase Inhibitors. J.Med.Chem. V. 66 14866 2023.
ISSN: ISSN 0022-2623
PubMed: 37905925
DOI: 10.1021/ACS.JMEDCHEM.3C01454
Page generated: Tue Jul 30 07:59:53 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy