Fluorine in PDB 2iko: Crystal Structure of Human Renin Complexed with Inhibitor

All present enzymatic activity of Crystal Structure of Human Renin Complexed with Inhibitor:
3.4.23.15;

The structure of Crystal Structure of Human Renin Complexed with Inhibitor, PDB code: 2iko was solved by I.Mochalkin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.90
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	140.885, 140.885, 140.885, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 22.9

The binding sites of Fluorine atom in the Crystal Structure of Human Renin Complexed with Inhibitor (pdb code 2iko). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Crystal Structure of Human Renin Complexed with Inhibitor, PDB code: 2iko:
Jump to Fluorine binding site number: 1; 2;

Fluorine binding site 1 out of 2 in the Crystal Structure of Human Renin Complexed with Inhibitor


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 Renin Complexed with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:28.2 occ:1.00 F1 A:7IG601 0.0 28.2 1.0 C13 A:7IG601 1.3 26.7 1.0 C14 A:7IG601 2.4 25.8 1.0 C18 A:7IG601 2.4 27.2 1.0 CB A:LEU116 3.5 33.8 1.0 CD1 A:LEU116 3.6 38.4 1.0 C15 A:7IG601 3.6 26.7 1.0 C17 A:7IG601 3.7 26.6 1.0 O A:HOH612 3.7 27.6 1.0 O A:HOH695 4.1 30.5 1.0 CG A:LEU116 4.1 35.2 1.0 C16 A:7IG601 4.1 27.4 1.0 O A:LEU116 4.3 32.0 1.0 CA A:LEU116 4.7 33.1 1.0 F2 A:7IG601 4.8 26.4 1.0 C A:LEU116 4.8 33.2 1.0 C19 A:7IG601 4.8 28.1 1.0 NE2 A:GLN14 4.9 32.0 1.0 CD2 A:LEU116 4.9 39.1 1.0

Fluorine binding site 2 out of 2 in the Crystal Structure of Human Renin Complexed with Inhibitor


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 Renin Complexed with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F601 b:26.4 occ:1.00 F2 A:7IG601 0.0 26.4 1.0 C17 A:7IG601 1.4 26.6 1.0 C18 A:7IG601 2.4 27.2 1.0 C16 A:7IG601 2.4 27.4 1.0 CB A:THR80 3.4 35.2 1.0 CG2 A:THR80 3.5 37.2 1.0 C13 A:7IG601 3.7 26.7 1.0 C15 A:7IG601 3.7 26.7 1.0 OG1 A:THR80 3.9 37.3 1.0 C14 A:7IG601 4.2 25.8 1.0 CB A:PRO113 4.7 33.1 1.0 CA A:THR80 4.7 35.4 1.0 F1 A:7IG601 4.8 28.2 1.0 O A:THR80 4.8 34.8 1.0 C19 A:7IG601 5.0 28.1 1.0

R.W.Sarver, J.Peevers, W.L.Cody, F.L.Ciske, J.Dyer, S.D.Emerson, J.C.Hagadorn, D.D.Holsworth, M.Jalaie, M.Kaufman, M.Mastronardi, P.Mcconnell, N.A.Powell, J.Quin, C.A.Van Huis, E.Zhang, I.Mochalkin. Binding Thermodynamics of Substituted Diaminopyrimidine Renin Inhibitors. Anal.Biochem. V. 360 30 2007.
ISSN: ISSN 0003-2697
PubMed: 17113558
DOI: 10.1016/J.AB.2006.10.017