Chlorine in PDB 3i3r: X-Ray Structure Dihydrofolate Reductase/Thymidylate Synthase From Babesia Bovis at 2.35A Resolution

All present enzymatic activity of X-Ray Structure Dihydrofolate Reductase/Thymidylate Synthase From Babesia Bovis at 2.35A Resolution:
2.1.1.45;

The structure of X-Ray Structure Dihydrofolate Reductase/Thymidylate Synthase From Babesia Bovis at 2.35A Resolution, PDB code: 3i3r was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), 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)	19.69 / 2.35
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	52.540, 83.480, 84.190, 119.00, 97.99, 100.69
R / Rfree (%)	20.2 / 25.1

The binding sites of Chlorine atom in the X-Ray Structure Dihydrofolate Reductase/Thymidylate Synthase From Babesia Bovis at 2.35A Resolution (pdb code 3i3r). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the X-Ray Structure Dihydrofolate Reductase/Thymidylate Synthase From Babesia Bovis at 2.35A Resolution, PDB code: 3i3r:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the X-Ray Structure Dihydrofolate Reductase/Thymidylate Synthase From Babesia Bovis at 2.35A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Structure Dihydrofolate Reductase/Thymidylate Synthase From Babesia Bovis at 2.35A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl601 b:33.5 occ:1.00 NH2 B:ARG374 3.3 31.6 1.0 NH1 A:ARG413 3.4 22.8 1.0 NE A:ARG248 3.6 36.7 1.0 NE B:ARG374 3.6 30.4 1.0 NH2 A:ARG413 3.8 23.1 1.0 CZ B:ARG374 3.9 30.8 1.0 CZ A:ARG413 4.0 22.2 1.0 NE B:ARG373 4.1 24.3 1.0 CG A:ARG248 4.2 35.5 1.0 NH2 A:ARG248 4.3 38.9 1.0 NH1 B:ARG373 4.3 24.3 1.0 CD A:ARG248 4.3 36.4 1.0 CZ A:ARG248 4.4 37.6 1.0 OG A:SER414 4.4 21.3 1.0 CB B:ARG373 4.5 25.0 1.0 CZ B:ARG373 4.7 24.8 1.0 CD B:ARG374 4.8 28.2 1.0 CB A:SER414 4.8 20.2 1.0 CG B:ARG374 4.9 25.9 1.0 CG B:ARG373 5.0 25.0 1.0

Chlorine binding site 2 out of 2 in the X-Ray Structure Dihydrofolate Reductase/Thymidylate Synthase From Babesia Bovis at 2.35A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of X-Ray Structure Dihydrofolate Reductase/Thymidylate Synthase From Babesia Bovis at 2.35A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl601 b:42.3 occ:1.00 NE B:ARG248 3.3 39.1 1.0 NH2 B:ARG248 3.5 39.5 1.0 NH1 B:ARG413 3.6 22.1 1.0 CZ B:ARG248 3.8 39.1 1.0 NH1 A:ARG373 3.8 28.8 1.0 NE A:ARG373 4.0 26.8 1.0 NH2 A:ARG374 4.0 34.3 1.0 NE A:ARG374 4.0 30.7 1.0 NH2 B:ARG413 4.0 21.6 1.0 CD B:ARG248 4.3 38.0 1.0 CZ B:ARG413 4.3 21.7 1.0 CZ A:ARG373 4.4 27.8 1.0 CB A:ARG373 4.4 26.7 1.0 OG B:SER414 4.4 21.2 1.0 CZ A:ARG374 4.5 33.2 1.0 CB B:SER414 4.7 20.6 1.0 NH1 B:ARG248 5.0 39.8 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