Chlorine in PDB 6psa: PIE12 D-Peptide Against Hiv Entry (in Complex with IQN17 Q577R Resistance Mutant)

The structure of PIE12 D-Peptide Against Hiv Entry (in Complex with IQN17 Q577R Resistance Mutant), PDB code: 6psa was solved by C.P.Hill, F.G.Whitby, M.Kay, M.Weinstock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	13.21 / 1.30
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	48.843, 48.843, 67.634, 90.00, 90.00, 120.00
R / Rfree (%)	17.6 / 21.7

The binding sites of Chlorine atom in the PIE12 D-Peptide Against Hiv Entry (in Complex with IQN17 Q577R Resistance Mutant) (pdb code 6psa). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the PIE12 D-Peptide Against Hiv Entry (in Complex with IQN17 Q577R Resistance Mutant), PDB code: 6psa:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the PIE12 D-Peptide Against Hiv Entry (in Complex with IQN17 Q577R Resistance Mutant)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of PIE12 D-Peptide Against Hiv Entry (in Complex with IQN17 Q577R Resistance Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl101 b:18.1 occ:0.19 HG1 A:THR33 2.1 16.7 1.0 OG1 A:THR33 2.9 13.9 1.0 HG21 A:THR33 3.0 16.8 1.0 HD12 A:LEU30 3.2 21.8 1.0 HB A:THR33 3.3 15.8 1.0 HD13 A:LEU30 3.4 21.8 1.0 CB A:THR33 3.4 13.1 1.0 CD1 A:LEU30 3.6 18.1 1.0 CG2 A:THR33 3.6 14.0 1.0 HD11 A:LEU30 3.9 21.8 1.0 HA A:LEU30 4.1 17.2 1.0 HG23 A:THR33 4.2 16.8 1.0 HG22 A:THR33 4.3 16.8 1.0 CA A:THR33 4.9 11.8 1.0 HD11 A:ILE37 4.9 20.1 1.0

Chlorine binding site 2 out of 2 in the PIE12 D-Peptide Against Hiv Entry (in Complex with IQN17 Q577R Resistance Mutant)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of PIE12 D-Peptide Against Hiv Entry (in Complex with IQN17 Q577R Resistance Mutant) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl102 b:19.8 occ:0.43 O A:HOH203 2.7 67.8 1.0 HG3 A:GLN16 2.8 17.6 1.0 HE21 A:GLN16 2.8 19.1 1.0 HA A:GLN16 2.9 16.2 1.0 HB2 A:GLN16 2.9 16.6 1.0 HD12 A:ILE19 3.0 20.9 1.0 HD13 A:ILE19 3.4 20.9 1.0 CB A:GLN16 3.4 13.8 1.0 CG A:GLN16 3.5 14.6 1.0 NE2 A:GLN16 3.5 15.8 1.0 CA A:GLN16 3.6 13.4 1.0 CD1 A:ILE19 3.7 17.3 1.0 CD A:GLN16 4.0 15.5 1.0 HG21 A:ILE19 4.1 18.8 1.0 HB A:ILE19 4.1 17.8 1.0 HD11 A:ILE19 4.2 20.9 1.0 HE22 A:GLN16 4.2 19.1 1.0 N A:GLN16 4.3 14.1 1.0 HG2 A:GLN16 4.3 17.6 1.0 HB3 A:GLN16 4.4 16.6 1.0 H A:GLN16 4.5 17.0 1.0 CB A:ILE19 4.8 14.8 1.0 CG1 A:ILE19 4.8 16.7 1.0 C A:GLN16 4.8 13.8 1.0 CG2 A:ILE19 4.8 15.6 1.0 HG23 A:ILE12 4.9 23.0 1.0 O A:GLN16 5.0 13.8 1.0

A.R.Smith, M.T.Weinstock, A.E.Siglin, F.G.Whitby, J.N.Francis, C.P.Hill, D.M.Eckert, M.J.Root, M.S.Kay. Characterization of Resistance to A Potent D-Peptide Hiv Entry Inhibitor. Retrovirology V. 16 28 2019.
ISSN: ESSN 1742-4690
PubMed: 31640718
DOI: 10.1186/S12977-019-0489-7