Chlorine in PDB 5fns: 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: 5fns 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)	47.41 / 1.79
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	103.621, 103.621, 55.838, 90.00, 90.00, 120.00
R / Rfree (%)	17.6 / 21.2

The binding sites of Chlorine atom in the Structure of the KEAP1 Kelch Domain in Complex with A Small Molecule Inhibitor. (pdb code 5fns). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Structure of the KEAP1 Kelch Domain in Complex with A Small Molecule Inhibitor., PDB code: 5fns:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 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:16.4 occ:0.96 CL1 A:XYY1614 0.0 16.4 1.0 C9 A:XYY1614 1.7 16.4 1.0 C8 A:XYY1614 2.7 16.4 1.0 C4 A:XYY1614 2.7 16.4 1.0 H3A A:XYY1614 2.7 17.3 1.0 H8 A:XYY1614 2.8 16.7 1.0 C3 A:XYY1614 3.1 17.8 1.0 O A:HOH2039 3.3 12.7 1.0 N2 A:XYY1614 3.5 16.4 1.0 O28 A:XYY1614 3.5 19.6 1.0 O A:HOH2084 3.6 13.2 1.0 CA A:GLY364 3.8 14.3 1.0 CB A:ALA556 3.9 17.9 1.0 C7 A:XYY1614 4.0 17.1 1.0 CG A:ARG415 4.0 15.7 1.0 C5 A:XYY1614 4.0 15.9 1.0 H3 A:XYY1614 4.0 17.1 1.0 CA A:GLY603 4.0 14.9 1.0 S26 A:XYY1614 4.1 19.0 1.0 O A:HOH2165 4.2 18.3 1.0 CB A:ARG415 4.4 14.9 1.0 CA A:ALA556 4.4 16.6 1.0 O A:HOH2275 4.5 14.8 1.0 CA A:ARG415 4.5 13.4 1.0 N A:GLY364 4.5 14.7 1.0 C6 A:XYY1614 4.5 18.7 1.0 H1 A:XYY1614 4.5 17.1 1.0 C1 A:XYY1614 4.6 17.9 1.0 H7 A:XYY1614 4.7 17.0 1.0 CD A:ARG415 4.7 18.5 1.0 H5 A:XYY1614 4.7 17.3 1.0 C A:GLY364 4.8 13.0 1.0 O A:HOH2225 4.8 22.0 1.0 N A:GLY603 4.9 15.2 1.0 O27 A:XYY1614 4.9 20.2 1.0 H1B A:XYY1614 4.9 17.3 1.0

Chlorine binding site 2 out of 2 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 2 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:Cl1615 b:25.1 occ:1.00 H29B A:XYY1614 2.9 19.2 1.0 O A:HOH2038 3.2 19.6 1.0 O A:HOH2051 3.2 45.6 1.0 ND2 A:ASN414 3.3 15.8 1.0 H3 A:XYY1614 3.5 17.1 1.0 ND2 A:ASN382 3.7 26.1 1.0 O A:HOH2086 3.8 29.6 1.0 H3A A:XYY1614 3.8 17.3 1.0 C29 A:XYY1614 3.9 19.1 1.0 C3 A:XYY1614 4.1 17.8 1.0 CD A:ARG380 4.1 22.4 1.0 CD A:ARG415 4.1 18.5 1.0 H29A A:XYY1614 4.2 18.6 1.0 CG A:ASN414 4.3 15.4 1.0 H29 A:XYY1614 4.3 19.0 1.0 OD1 A:ASN414 4.3 14.4 1.0 OD1 A:ASN382 4.5 30.8 1.0 NE A:ARG415 4.5 19.8 1.0 CG A:ARG415 4.5 15.7 1.0 NE A:ARG380 4.5 27.0 1.0 CG A:ASN382 4.6 28.4 1.0 NH1 A:ARG415 4.8 23.0 1.0 CZ A:ARG415 4.8 23.3 1.0 O28 A:XYY1614 4.9 19.6 1.0 S26 A:XYY1614 4.9 19.0 1.0 N2 A:XYY1614 4.9 16.4 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