Chlorine in PDB 5jed: Apo-Structure of Humanised Rada-Mutant HUMRADA28

The structure of Apo-Structure of Humanised Rada-Mutant HUMRADA28, PDB code: 5jed 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)	37.72 / 1.33
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.771, 72.100, 41.927, 90.00, 115.89, 90.00
R / Rfree (%)	13.5 / 17.1

The binding sites of Chlorine atom in the Apo-Structure of Humanised Rada-Mutant HUMRADA28 (pdb code 5jed). 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 HUMRADA28, PDB code: 5jed:

Chlorine binding site 1 out of 1 in the Apo-Structure of Humanised Rada-Mutant HUMRADA28


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 HUMRADA28 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:26.3 occ:1.00 NE2 A:HIS269 3.2 20.8 1.0 O A:HOH672 3.2 34.4 1.0 N A:ALA297 3.2 19.3 1.0 CB A:ALA297 3.8 22.1 1.0 CA A:ALA297 3.8 18.6 1.0 C A:ALA297 3.8 18.9 1.0 CG2 A:THR310 3.9 15.9 1.0 CD2 A:HIS269 4.0 18.9 1.0 N A:THR310 4.0 14.8 1.0 CB A:SER296 4.1 23.1 1.0 CE1 A:HIS269 4.2 20.5 1.0 C A:SER296 4.2 21.7 1.0 CB A:LEU265 4.2 14.3 1.0 CD1 A:LEU265 4.3 19.9 1.0 CD2 A:LEU265 4.3 17.5 1.0 CA A:SER296 4.3 21.6 1.0 O A:ALA297 4.4 24.2 1.0 CG A:LEU265 4.5 16.8 1.0 O A:HOH589 4.8 26.0 1.0 OG A:SER296 4.9 22.4 1.0 CA A:THR310 4.9 13.8 1.0 CB A:THR310 4.9 14.2 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