Chlorine in PDB 5jec: Apo-Structure of Humanised Rada-Mutant HUMRADA33F

The structure of Apo-Structure of Humanised Rada-Mutant HUMRADA33F, PDB code: 5jec 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)	78.59 / 2.34
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	90.750, 90.750, 102.510, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 23.9

The binding sites of Chlorine atom in the Apo-Structure of Humanised Rada-Mutant HUMRADA33F (pdb code 5jec). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Apo-Structure of Humanised Rada-Mutant HUMRADA33F, PDB code: 5jec:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Apo-Structure of Humanised Rada-Mutant HUMRADA33F


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 HUMRADA33F within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:83.0 occ:1.00 OG1 A:THR228 3.2 37.0 1.0 O A:ARG230 3.2 41.6 1.0 NZ A:LYS167 3.5 44.7 1.0 CD2 A:LEU225 3.6 33.9 1.0 CB A:THR228 4.0 34.5 1.0 C A:ARG230 4.0 42.7 1.0 CD1 A:LEU225 4.0 31.2 1.0 CG A:LEU225 4.2 31.6 1.0 N A:ARG230 4.3 46.0 1.0 CB A:ARG230 4.4 47.2 1.0 CA A:ARG230 4.4 45.1 1.0 CE A:LYS167 4.4 48.4 1.0 CB A:LEU225 4.5 28.6 1.0 CG2 A:THR228 4.6 31.0 1.0 N A:PRO231 5.0 35.1 1.0

Chlorine binding site 2 out of 2 in the Apo-Structure of Humanised Rada-Mutant HUMRADA33F


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Apo-Structure of Humanised Rada-Mutant HUMRADA33F within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:28.5 occ:1.00 O B:HOH521 3.1 25.8 1.0 NE2 A:GLN258 3.2 19.6 1.0 NE A:ARG257 3.2 26.1 1.0 O A:HOH532 3.3 25.9 1.0 NH2 A:ARG257 3.5 23.7 1.0 CA A:GLN258 3.7 25.6 1.0 CB A:GLN258 3.7 25.9 1.0 CZ A:ARG257 3.8 39.7 1.0 N A:GLN258 3.9 25.9 1.0 CG A:LEU305 4.0 39.2 1.0 CA A:LEU305 4.1 34.4 1.0 C A:ARG257 4.2 29.1 1.0 CG A:ARG257 4.2 27.0 1.0 CD A:GLN258 4.3 27.5 1.0 CD A:ARG257 4.3 23.9 1.0 CB A:LEU305 4.3 34.0 1.0 O A:ARG257 4.3 28.9 1.0 O A:ILE304 4.3 46.7 1.0 CD2 A:LEU305 4.4 41.2 1.0 NE2 B:HIS210 4.4 27.7 1.0 CB A:ARG257 4.5 22.5 1.0 CG A:GLN258 4.5 26.5 1.0 CD2 A:LEU261 4.5 33.1 1.0 N A:ALA306 4.6 30.2 1.0 C A:LEU305 4.7 35.6 1.0 O A:ALA306 4.8 31.6 1.0 O A:LEU254 4.8 32.4 1.0

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