Chlorine in PDB 6cxk: E. Coli Dhfr Substrate Complex with Dihydrofolate

All present enzymatic activity of E. Coli Dhfr Substrate Complex with Dihydrofolate:
1.5.1.3;

The structure of E. Coli Dhfr Substrate Complex with Dihydrofolate, PDB code: 6cxk was solved by H.Cao, J.Rodrigues, J.Benach, A.Frommelt, L.Morisco, J.Koss, E.Shakhnovich, J.Skolnick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.95 / 1.11
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	33.698, 51.525, 77.421, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 19.6

The structure of E. Coli Dhfr Substrate Complex with Dihydrofolate also contains other interesting chemical elements:

Magnesium

(Mg)

8 atoms

The binding sites of Chlorine atom in the E. Coli Dhfr Substrate Complex with Dihydrofolate (pdb code 6cxk). 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 E. Coli Dhfr Substrate Complex with Dihydrofolate, PDB code: 6cxk:

Chlorine binding site 1 out of 1 in the E. Coli Dhfr Substrate Complex with Dihydrofolate


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of E. Coli Dhfr Substrate Complex with Dihydrofolate within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl209 b:14.5 occ:1.00 H A:GLY96 2.3 12.2 1.0 H A:THR46 2.5 15.7 1.0 HB3 A:HIS45 2.6 25.3 0.6 HG1 A:THR46 2.7 19.3 1.0 HA3 A:GLY43 2.7 13.3 1.0 HB3 A:HIS45 2.7 25.2 0.4 O A:HOH452 2.9 22.0 1.0 H A:HIS45 3.1 17.4 1.0 N A:GLY96 3.1 10.2 1.0 O A:HOH404 3.2 30.2 1.0 N A:THR46 3.3 13.1 1.0 CA A:GLY43 3.4 11.1 1.0 H A:GLY43 3.4 11.8 1.0 OG1 A:THR46 3.4 16.1 1.0 HA3 A:GLY96 3.4 12.5 1.0 C A:GLY43 3.4 11.9 1.0 CB A:HIS45 3.5 21.1 0.6 HB A:THR46 3.5 15.1 1.0 CB A:HIS45 3.6 21.0 0.4 N A:HIS45 3.6 14.5 1.0 O A:HOH453 3.6 29.1 1.0 O A:GLY43 3.8 10.7 1.0 N A:GLY43 3.8 9.8 1.0 HB2 A:HIS45 3.8 25.3 0.6 O A:HOH431 3.8 24.0 1.0 CA A:GLY96 3.8 10.4 1.0 HB2 A:HIS45 3.9 25.2 0.4 CB A:THR46 3.9 12.6 1.0 CA A:HIS45 3.9 15.7 0.6 CA A:HIS45 3.9 15.7 0.4 N A:ARG44 3.9 13.2 1.0 HG23 A:VAL99 4.0 17.6 1.0 H A:ARG44 4.1 15.8 1.0 C A:GLY95 4.1 11.0 1.0 C A:HIS45 4.1 14.7 1.0 O A:GLY95 4.1 11.6 1.0 HG21 A:VAL99 4.1 17.6 1.0 HA2 A:GLY43 4.2 13.3 1.0 CA A:THR46 4.2 11.8 1.0 O A:HOH460 4.5 19.7 1.0 C A:ARG44 4.5 15.1 1.0 CG2 A:VAL99 4.5 14.6 1.0 HA2 A:GLY96 4.6 12.5 1.0 CG A:HIS45 4.6 24.8 0.6 C A:GLY96 4.7 9.5 1.0 HB A:VAL99 4.7 12.4 1.0 CG A:HIS45 4.7 24.9 0.4 HA A:THR46 4.7 14.2 1.0 SD A:MET16 4.7 48.9 0.4 HG3 A:MET16 4.8 54.0 0.6 ND1 A:HIS45 4.8 27.0 0.6 CA A:ARG44 4.8 14.2 1.0 H A:TRP47 4.8 14.9 1.0 HA A:HIS45 4.9 18.8 0.4 H A:VAL99 4.9 11.5 1.0

H.Cao, M.Gao, H.Zhou, J.Skolnick. The Crystal Structure of A Tetrahydrofolate-Bound Dihydrofolate Reductase Reveals the Origin of Slow Product Release. Commun Biol V. 1 226 2018.
ISSN: ESSN 2399-3642
PubMed: 30564747
DOI: 10.1038/S42003-018-0236-Y