Iron in PDB 5j6d: Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors

All present enzymatic activity of Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors:
1.14.16.4;

The structure of Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors, PDB code: 5j6d was solved by A.J.Stein, D.R.Goldberg, S.De Lombaert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.726, 63.561, 156.468, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 24.8

The binding sites of Iron atom in the Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors (pdb code 5j6d). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors, PDB code: 5j6d:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:23.1 occ:1.00 NE2 A:HIS277 2.1 22.7 1.0 OE2 A:GLU317 2.1 27.6 1.0 NE2 A:HIS272 2.2 25.3 1.0 O2 A:TRS502 2.2 24.9 1.0 O3 A:TRS502 2.2 25.6 1.0 N A:TRS502 2.2 24.3 1.0 C A:TRS502 2.9 24.8 1.0 CD A:GLU317 3.0 28.1 1.0 CE1 A:HIS272 3.0 26.5 1.0 C3 A:TRS502 3.0 26.1 1.0 CE1 A:HIS277 3.0 24.5 1.0 C2 A:TRS502 3.0 24.8 1.0 CD2 A:HIS277 3.1 24.2 1.0 OE1 A:GLU317 3.2 27.7 1.0 CD2 A:HIS272 3.2 25.3 1.0 ND1 A:HIS277 4.2 24.6 1.0 OE2 A:GLU273 4.2 24.8 1.0 ND1 A:HIS272 4.2 25.9 1.0 CG A:HIS277 4.2 24.6 1.0 CG A:HIS272 4.3 25.9 1.0 C1 A:TRS502 4.3 25.0 1.0 C5 A:6H5504 4.4 27.5 1.0 CG A:GLU317 4.4 26.3 1.0 OH A:TYR312 4.6 30.7 1.0 CZ A:PHE250 4.7 25.8 1.0 CB A:ALA332 4.7 27.5 1.0 C4 A:6H5504 4.7 28.8 1.0 N1 A:6H5504 4.8 28.8 1.0

Iron binding site 2 out of 2 in the Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:48.5 occ:1.00 OE2 B:GLU317 1.9 43.9 1.0 O2 B:TRS502 2.1 48.5 1.0 O1 B:TRS502 2.2 55.4 1.0 NE2 B:HIS272 2.2 61.7 1.0 NE2 B:HIS277 2.4 45.2 1.0 N B:TRS502 2.4 50.0 1.0 C B:TRS502 2.9 46.1 1.0 C2 B:TRS502 3.0 49.0 1.0 CD2 B:HIS277 3.0 46.6 1.0 CD B:GLU317 3.0 48.4 1.0 C1 B:TRS502 3.0 49.2 1.0 CE1 B:HIS272 3.1 60.7 1.0 CD2 B:HIS272 3.2 61.3 1.0 OE1 B:GLU317 3.4 46.7 1.0 CE1 B:HIS277 3.5 47.0 1.0 OE2 B:GLU273 4.1 61.9 1.0 CG B:HIS277 4.2 47.3 1.0 ND1 B:HIS272 4.2 58.2 1.0 CG B:GLU317 4.3 48.6 1.0 CG B:HIS272 4.3 58.0 1.0 C28 B:6H5504 4.3 57.4 1.0 C3 B:TRS502 4.4 46.7 1.0 ND1 B:HIS277 4.4 47.1 1.0 CZ B:PHE250 4.6 42.9 1.0 C29 B:6H5504 4.7 59.2 1.0 CB B:ALA332 4.9 58.4 1.0 N1 B:6H5504 4.9 50.5 1.0 CD B:GLU273 4.9 60.6 1.0 OE1 B:GLU273 5.0 59.5 1.0

D.R.Goldberg, S.De Lombaert, R.Aiello, P.Bourassa, N.Barucci, Q.Zhang, V.Paralkar, A.J.Stein, J.Valentine, W.Zavadoski. Discovery of Acyl Guanidine Tryptophan Hydroxylase-1 Inhibitors. Bioorg.Med.Chem.Lett. V. 26 2855 2016.
ISSN: ESSN 1464-3405
PubMed: 27146606
DOI: 10.1016/J.BMCL.2016.04.057