Chlorine in PDB 4ch9: Crystal Structure of the Human KLHL3 Kelch Domain in Complex with A WNK4 Peptide

All present enzymatic activity of Crystal Structure of the Human KLHL3 Kelch Domain in Complex with A WNK4 Peptide:
2.7.11.1;

The structure of Crystal Structure of the Human KLHL3 Kelch Domain in Complex with A WNK4 Peptide, PDB code: 4ch9 was solved by F.J.Sorrell, F.R.Schumacher, T.Kurz, D.R.Alessi, J.Newman, S.Goubin, R.Chalk, J.Kopec, C.Tallant, E.Williams, T.Krojer, F.Von Delft, C.H.Arrowsmith, A.M.Edwards, C.Bountra, A.Bullock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	73.402 / 1.84
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	45.330, 84.760, 146.790, 90.00, 90.00, 90.00
R / Rfree (%)	14.39 / 18.4

The binding sites of Chlorine atom in the Crystal Structure of the Human KLHL3 Kelch Domain in Complex with A WNK4 Peptide (pdb code 4ch9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Human KLHL3 Kelch Domain in Complex with A WNK4 Peptide, PDB code: 4ch9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of the Human KLHL3 Kelch Domain in Complex with A WNK4 Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of the Human KLHL3 Kelch Domain in Complex with A WNK4 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1588 b:19.4 occ:1.00 O A:HOH2083 3.1 7.5 1.0 OG A:SER385 3.1 9.4 1.0 NH1 A:ARG339 3.2 13.6 1.0 NE A:ARG360 3.2 15.3 1.0 NH2 A:ARG360 3.4 16.6 1.0 CB A:SER385 3.5 13.5 1.0 CD A:ARG339 3.7 11.2 1.0 CZ A:ARG360 3.8 10.8 1.0 CD2 A:PHE402 3.9 11.2 1.0 CG2 A:THR386 4.0 8.4 1.0 CA C:PRO561 4.0 11.1 1.0 CG A:ARG360 4.2 11.3 1.0 CZ A:ARG339 4.2 13.1 1.0 CD A:ARG360 4.3 12.5 1.0 NE A:ARG339 4.4 11.9 1.0 CB A:PHE402 4.5 8.0 1.0 C A:SER385 4.5 7.3 1.0 O A:SER385 4.5 9.1 1.0 O C:GLU560 4.6 9.6 1.0 CB C:PRO561 4.6 16.1 1.0 CA A:SER385 4.6 9.4 1.0 CG A:PHE402 4.6 8.3 1.0 OG1 A:THR386 4.7 9.4 1.0 N C:PRO561 4.7 9.6 1.0 CE2 A:PHE402 4.7 21.2 1.0 N C:GLU562 4.7 12.6 1.0 N A:THR386 4.9 6.4 1.0 C C:PRO561 4.9 8.4 1.0 CB A:THR386 4.9 11.8 1.0 C C:GLU560 5.0 13.1 1.0 CG A:ARG339 5.0 10.0 1.0 CG C:PRO561 5.0 17.1 1.0 CD1 A:PHE355 5.0 14.9 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of the Human KLHL3 Kelch Domain in Complex with A WNK4 Peptide


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of the Human KLHL3 Kelch Domain in Complex with A WNK4 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1589 b:19.4 occ:1.00 O B:HOH2087 3.0 10.3 1.0 OG B:SER385 3.1 7.4 1.0 NH1 B:ARG339 3.2 11.7 1.0 NE B:ARG360 3.2 12.0 1.0 NH2 B:ARG360 3.4 15.0 1.0 CB B:SER385 3.5 11.0 1.0 CD B:ARG339 3.7 7.6 1.0 CD2 B:PHE402 3.8 9.6 1.0 CZ B:ARG360 3.8 15.5 1.0 CA D:PRO561 4.0 10.1 1.0 CG2 B:THR386 4.1 10.2 1.0 CG B:ARG360 4.2 8.9 1.0 CZ B:ARG339 4.2 11.3 1.0 CD B:ARG360 4.3 11.9 1.0 CB B:PHE402 4.4 8.4 1.0 NE B:ARG339 4.4 9.9 1.0 C B:SER385 4.5 8.2 1.0 O B:SER385 4.5 7.8 1.0 O D:GLU560 4.5 11.9 1.0 CG B:PHE402 4.5 10.2 1.0 CA B:SER385 4.6 11.7 1.0 CE2 B:PHE402 4.6 10.1 1.0 N D:GLU562 4.7 13.1 1.0 OG1 B:THR386 4.7 10.1 1.0 N D:PRO561 4.7 7.8 1.0 CB D:PRO561 4.7 10.6 1.0 C D:PRO561 4.9 14.1 1.0 N B:THR386 4.9 7.9 1.0 CB B:PHE355 4.9 8.3 1.0 C D:GLU560 4.9 11.7 1.0 CB B:THR386 5.0 10.6 1.0 CD1 B:PHE355 5.0 10.1 1.0 O B:PHE402 5.0 9.1 1.0

F.Schumacher, F.J.Sorrell, D.R.Alessi, A.N.Bullock, T.Kurz. Structural and Biochemical Characterisation of the KLHL3- Wnk Kinase Interaction Important in Blood Pressure Regulation. Biochem.J. V. 460 237 2014.
ISSN: ISSN 0264-6021
PubMed: 24641320
DOI: 10.1042/BJ20140153