Chlorine in PDB 5fnq: Structure of the KEAP1 Kelch Domain in Complex with A Small Molecule Inhibitor.

The structure of Structure of the KEAP1 Kelch Domain in Complex with A Small Molecule Inhibitor., PDB code: 5fnq was solved by T.G.Davies, W.E.Wixted, J.E.Coyle, C.Griffiths-Jones, K.Hearn, R.Mcmenamin, D.Norton, S.J.Rich, C.Richardson, G.Saxty, H.M.G.Willems, A.J.Woolford, J.E.Cottom, J.Kou, J.G.Yonchuk, H.G.Feldser, Y.Sanchez, J.P.Foley, B.J.Bolognese, G.Logan, P.L.Podolin, H.Yan, J.F.Callahan, T.D.Heightman, J.K.Kerns, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.87 / 1.91
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	103.625, 103.625, 56.027, 90.00, 90.00, 120.00
R / Rfree (%)	17.8 / 21.5

The binding sites of Chlorine atom in the Structure of the KEAP1 Kelch Domain in Complex with A Small Molecule Inhibitor. (pdb code 5fnq). 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 Structure of the KEAP1 Kelch Domain in Complex with A Small Molecule Inhibitor., PDB code: 5fnq:

Chlorine binding site 1 out of 1 in the Structure of the KEAP1 Kelch Domain in Complex with A Small Molecule Inhibitor.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of the KEAP1 Kelch Domain in Complex with A Small Molecule Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1614 b:18.6 occ:0.77 CL1 A:S0W1614 0.0 18.6 0.8 C9 A:S0W1614 1.7 17.9 0.8 C8 A:S0W1614 2.7 15.8 0.8 C11 A:S0W1614 2.7 17.7 0.8 H8 A:S0W1614 2.8 17.1 0.8 H11 A:S0W1614 2.8 17.8 0.8 O A:HOH2039 3.3 13.3 1.0 O A:HOH2089 3.7 15.0 1.0 CB A:ALA556 3.7 17.0 1.0 CA A:GLY603 3.9 14.6 1.0 CA A:GLY364 4.0 13.8 1.0 C7 A:S0W1614 4.0 17.5 0.8 C12 A:S0W1614 4.0 17.5 0.8 O A:HOH2167 4.0 22.7 1.0 CG A:ARG415 4.1 17.0 1.0 CA A:ALA556 4.1 16.0 1.0 O A:HOH2277 4.2 14.8 1.0 O A:HOH2309 4.4 35.2 1.0 O A:HOH2087 4.4 38.6 1.0 C6 A:S0W1614 4.5 19.8 0.8 O A:HOH2230 4.6 19.9 1.0 CB A:ARG415 4.6 14.2 1.0 N A:GLY603 4.6 14.9 1.0 N A:GLY364 4.7 14.3 1.0 CA A:ARG415 4.7 12.5 1.0 H7 A:S0W1614 4.7 17.3 0.8 H12 A:S0W1614 4.7 18.3 0.8 NE A:ARG415 4.9 24.7 1.0 C A:ALA556 4.9 17.0 1.0 CD A:ARG415 4.9 20.7 1.0 C A:GLY603 4.9 13.9 1.0 C A:GLY364 5.0 13.1 1.0

T.G.Davies, W.E.Wixted, J.E.Coyle, C.Griffiths-Jones, K.Hearn, R.L.Mcmenamin, D.Norton, S.J.Rich, C.Richardson, G.Saxty, H.M.G.Willems, A.J.Woolford, J.E.Cottom, J.Kou, J.G.Yonchuk, H.G.Feldser, Y.Sanchez, J.P.Foley, B.J.Bolognese, G.A.Logan, P.L.Podolin, H.Yan, J.F.Callahan, T.D.Heightman, J.K.Kerns. Mono-Acidic Inhibitors of the Kelch-Like Ech-Associated Protein 1 : Nuclear Factor Erythroid 2-Related Factor 2 (KEAP1:NRF2) Protein-Protein Interaction with High Cell Potency Identified By Fragment-Based Discovery. J.Med.Chem. V. 59 3991 2016.
ISSN: ISSN 0022-2623
PubMed: 27031670
DOI: 10.1021/ACS.JMEDCHEM.6B00228