Chlorine in PDB 3nrr: Co-Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis with Dump, Raltitrexed and Nadp

All present enzymatic activity of Co-Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis with Dump, Raltitrexed and Nadp:
2.1.1.45;

The structure of Co-Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis with Dump, Raltitrexed and Nadp, PDB code: 3nrr was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.94 / 1.80
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	51.330, 83.830, 83.920, 119.61, 102.04, 90.26
R / Rfree (%)	19.4 / 23.6

The binding sites of Chlorine atom in the Co-Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis with Dump, Raltitrexed and Nadp (pdb code 3nrr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Co-Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis with Dump, Raltitrexed and Nadp, PDB code: 3nrr:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Co-Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis with Dump, Raltitrexed and Nadp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Co-Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis with Dump, Raltitrexed and Nadp within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl513 b:28.0 occ:1.00 O A:HOH713 2.6 14.2 1.0 O A:ALA433 2.8 8.9 1.0 O A:HOH596 2.9 16.4 1.0 O A:HOH922 2.9 24.8 1.0 C A:ALA433 3.6 8.8 1.0 CA A:ALA433 3.7 9.6 1.0 N A:GLN437 3.7 12.9 1.0 CB A:GLN437 3.8 12.9 1.0 CB A:ALA433 3.9 10.0 1.0 CB A:ALA436 4.1 10.5 1.0 CD1 A:LEU443 4.1 19.0 1.0 CA A:GLN437 4.1 13.5 1.0 CG A:LEU443 4.2 15.8 1.0 CD1 A:LEU479 4.2 11.8 1.0 C A:ALA436 4.5 11.8 1.0 O A:HOH984 4.5 23.1 1.0 O A:HOH563 4.5 11.5 1.0 OE1 A:GLN437 4.6 14.0 1.0 CD2 A:LEU443 4.7 17.0 1.0 N A:MET434 4.8 7.8 1.0 CA A:ALA436 4.8 11.1 1.0 O A:LEU441 4.9 13.6 1.0 O A:HOH1000 4.9 35.1 1.0 O A:HOH663 5.0 24.7 1.0

Chlorine binding site 2 out of 2 in the Co-Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis with Dump, Raltitrexed and Nadp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Co-Crystal Structure of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis with Dump, Raltitrexed and Nadp within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl514 b:54.6 occ:1.00 O B:HOH589 4.9 27.4 1.0

D.W.Begley, T.E.Edwards, A.C.Raymond, E.R.Smith, R.C.Hartley, J.Abendroth, B.Sankaran, D.D.Lorimer, P.J.Myler, B.L.Staker, L.J.Stewart. Inhibitor-Bound Complexes of Dihydrofolate Reductase-Thymidylate Synthase From Babesia Bovis. Acta Crystallogr.,Sect.F V. 67 1070 2011.
ISSN: ESSN 1744-3091
PubMed: 21904052
DOI: 10.1107/S1744309111029009