Fluorine in PDB 2i4q: Human Renin/PF02342674 Complex

All present enzymatic activity of Human Renin/PF02342674 Complex:
3.4.23.15;

The structure of Human Renin/PF02342674 Complex, PDB code: 2i4q was solved by D.D.Holsworth, M.Jalaie, E.Zhang, P.Mcconnell, I.Mochalkin, B.C.Finzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.00 / 2.30
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	141.898, 141.898, 141.898, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 26.1

The binding sites of Fluorine atom in the Human Renin/PF02342674 Complex (pdb code 2i4q). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Human Renin/PF02342674 Complex, PDB code: 2i4q:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Human Renin/PF02342674 Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Human Renin/PF02342674 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F336 b:38.1 occ:1.00 F34 A:UA4336 0.0 38.1 1.0 C31 A:UA4336 1.3 38.6 1.0 C32 A:UA4336 2.3 37.4 1.0 C30 A:UA4336 2.4 39.5 1.0 CB A:THR80 3.3 36.4 1.0 CG2 A:THR80 3.5 36.7 1.0 C29 A:UA4336 3.6 40.1 1.0 C27 A:UA4336 3.7 37.1 1.0 OG1 A:THR80 3.9 36.7 1.0 O A:HOH340 3.9 50.3 1.0 C28 A:UA4336 4.0 38.8 1.0 CB A:PRO113 4.5 29.8 1.0 O A:THR80 4.5 36.6 1.0 CA A:THR80 4.6 36.0 1.0 F33 A:UA4336 4.7 40.7 1.0 C18 A:UA4336 4.9 35.5 1.0 O A:HOH338 5.0 33.5 1.0

Fluorine binding site 2 out of 4 in the Human Renin/PF02342674 Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Human Renin/PF02342674 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F336 b:40.7 occ:1.00 F33 A:UA4336 0.0 40.7 1.0 C29 A:UA4336 1.3 40.1 1.0 C30 A:UA4336 2.3 39.5 1.0 C28 A:UA4336 2.3 38.8 1.0 O A:HOH423 3.2 48.3 1.0 O A:HOH411 3.4 45.0 1.0 C27 A:UA4336 3.5 37.1 1.0 C31 A:UA4336 3.6 38.6 1.0 CD1 A:LEU116 3.9 33.3 1.0 C32 A:UA4336 4.1 37.4 1.0 CB A:LEU116 4.4 31.2 1.0 CG A:LEU116 4.7 32.1 1.0 F34 A:UA4336 4.7 38.1 1.0 O A:HOH340 4.7 50.3 1.0 C18 A:UA4336 4.7 35.5 1.0 O21 A:UA4336 4.8 35.0 1.0 C35 A:UA4336 4.9 35.6 1.0

Fluorine binding site 3 out of 4 in the Human Renin/PF02342674 Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Human Renin/PF02342674 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:F336 b:44.8 occ:1.00 F34 B:UA4336 0.0 44.8 1.0 C31 B:UA4336 1.3 43.2 1.0 C32 B:UA4336 2.3 42.1 1.0 C30 B:UA4336 2.4 42.6 1.0 CD1 B:LEU116 3.2 44.8 1.0 C29 B:UA4336 3.6 42.4 1.0 C27 B:UA4336 3.7 40.9 1.0 O B:HOH415 3.7 40.0 1.0 C28 B:UA4336 4.1 41.5 1.0 O B:HOH366 4.1 42.4 1.0 CG B:LEU116 4.4 44.7 1.0 CB B:LEU116 4.4 44.6 1.0 F33 B:UA4336 4.7 42.8 1.0 O B:HOH360 4.7 47.6 1.0 C18 B:UA4336 4.9 39.4 1.0

Fluorine binding site 4 out of 4 in the Human Renin/PF02342674 Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Human Renin/PF02342674 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:F336 b:42.8 occ:1.00 F33 B:UA4336 0.0 42.8 1.0 C29 B:UA4336 1.3 42.4 1.0 C28 B:UA4336 2.2 41.5 1.0 C30 B:UA4336 2.3 42.6 1.0 CB B:THR80 2.9 57.6 1.0 CG2 B:THR80 3.0 57.8 1.0 OG1 B:THR80 3.4 58.0 1.0 C27 B:UA4336 3.4 40.9 1.0 C31 B:UA4336 3.6 43.2 1.0 C32 B:UA4336 4.0 42.1 1.0 CB B:PRO113 4.1 45.3 1.0 CA B:THR80 4.3 56.9 1.0 CG B:PRO113 4.4 45.5 1.0 C18 B:UA4336 4.7 39.4 1.0 O17 B:UA4336 4.7 38.7 1.0 F34 B:UA4336 4.7 44.8 1.0 O B:HOH360 4.7 47.6 1.0 C B:THR80 4.8 57.1 1.0 C14 B:UA4336 4.9 38.3 1.0

N.A.Powell, F.L.Ciske, C.Cai, D.D.Holsworth, K.Mennen, C.A.Van Huis, M.Jalaie, J.Day, M.Mastronardi, P.Mcconnell, I.Mochalkin, E.Zhang, M.J.Ryan, J.Bryant, W.Collard, S.Ferreira, C.Gu, R.Collins, J.J.Edmunds. Rational Design of 6-(2,4-Diaminopyrimidinyl)-1,4-Benzoxazin-3-Ones As Small Molecule Renin Inhibitors. Bioorg.Med.Chem. V. 15 5912 2007.
ISSN: ISSN 0968-0896
PubMed: 17574423
DOI: 10.1016/J.BMC.2007.05.069