Chlorine in PDB 5j4l: Apo-Structure of Humanised Rada-Mutant HUMRADA22F

The structure of Apo-Structure of Humanised Rada-Mutant HUMRADA22F, PDB code: 5j4l was solved by G.Fischer, M.Marsh, T.Moschetti, T.Sharpe, D.Scott, M.Morgan, H.Ng, J.Skidmore, A.Venkitaraman, C.Abell, T.L.Blundell, M.Hyvonen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.76 / 1.13
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.481, 61.060, 87.911, 90.00, 90.00, 90.00
R / Rfree (%)	12.3 / 14.5

The binding sites of Chlorine atom in the Apo-Structure of Humanised Rada-Mutant HUMRADA22F (pdb code 5j4l). 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 Apo-Structure of Humanised Rada-Mutant HUMRADA22F, PDB code: 5j4l:

Chlorine binding site 1 out of 1 in the Apo-Structure of Humanised Rada-Mutant HUMRADA22F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Apo-Structure of Humanised Rada-Mutant HUMRADA22F within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:14.7 occ:1.00 H A:GLY143 2.5 11.7 1.0 H A:THR145 2.6 11.1 1.0 H A:GLN146 2.7 10.2 1.0 HG2 A:GLN146 3.0 13.8 1.0 HB A:THR145 3.1 14.2 1.0 HA2 A:GLY143 3.1 11.8 1.0 O A:HOH737 3.1 54.0 1.0 O A:HOH677 3.1 16.1 1.0 O A:HOH689 3.2 34.8 1.0 N A:GLY143 3.2 9.7 1.0 N A:THR145 3.3 9.3 1.0 H A:LYS144 3.3 11.2 0.5 H A:LYS144 3.3 11.2 0.5 C A:GLY143 3.4 9.7 1.0 CA A:GLY143 3.4 9.8 1.0 HA2 A:GLY141 3.4 16.6 1.0 N A:LYS144 3.4 9.3 1.0 N A:GLN146 3.5 8.5 1.0 HG2 A:LYS144 3.6 16.6 0.5 H A:GLY141 3.7 16.4 1.0 HG2 A:LYS144 3.8 14.1 0.5 CG A:GLN146 3.8 11.5 1.0 CB A:THR145 3.9 11.9 1.0 HB2 A:GLN146 3.9 12.1 1.0 CA A:THR145 4.0 9.5 1.0 O A:GLY143 4.0 9.1 1.0 CA A:GLY141 4.0 13.8 1.0 C A:GLY141 4.0 12.8 1.0 HG3 A:GLN146 4.2 13.8 1.0 C A:LYS144 4.2 9.3 1.0 N A:GLY141 4.2 13.6 1.0 C A:THR145 4.2 9.2 1.0 HE21 A:GLN146 4.2 19.1 1.0 N A:SER142 4.2 11.5 1.0 CB A:GLN146 4.3 10.1 1.0 H A:SER142 4.3 13.8 1.0 HG3 A:LYS144 4.3 16.6 0.5 CA A:LYS144 4.3 9.4 0.5 CA A:LYS144 4.3 10.0 0.5 HA3 A:GLY143 4.3 11.8 1.0 CG A:LYS144 4.4 13.8 0.5 HG3 A:LYS144 4.4 14.1 0.5 C A:SER142 4.5 10.4 1.0 CG A:LYS144 4.5 11.8 0.5 O A:GLY141 4.5 13.7 1.0 OG1 A:THR145 4.5 13.6 1.0 CA A:GLN146 4.5 8.8 1.0 HD13 A:ILE342 4.7 19.7 1.0 HZ2 A:LYS144 4.8 14.1 0.5 O A:HOH647 4.8 17.7 1.0 HA3 A:GLY141 4.9 16.6 1.0 NE2 A:GLN146 4.9 15.9 1.0 HA A:THR145 4.9 11.4 1.0 HG A:SER142 4.9 15.2 1.0 HD11 A:ILE342 4.9 19.7 1.0 CD A:GLN146 4.9 13.6 1.0 H A:LEU147 4.9 9.4 1.0 CA A:SER142 4.9 10.9 1.0 HG22 A:THR145 5.0 15.1 1.0 CB A:LYS144 5.0 12.1 0.5

T.Moschetti, T.Sharpe, G.Fischer, M.E.Marsh, H.K.Ng, M.Morgan, D.E.Scott, T.L.Blundell, A.R Venkitaraman, J.Skidmore, C.Abell, M.Hyvonen. Engineering Archeal Surrogate Systems For the Development of Protein-Protein Interaction Inhibitors Against Human RAD51. J.Mol.Biol. V. 428 4589 2016.
ISSN: ESSN 1089-8638
PubMed: 27725183
DOI: 10.1016/J.JMB.2016.10.009