Chlorine in PDB 2d0k: Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase

All present enzymatic activity of Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase:
1.5.1.3;

The structure of Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase, PDB code: 2d0k was solved by K.Katayanagi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	79.580, 56.690, 85.140, 90.00, 106.81, 90.00
R / Rfree (%)	20.5 / 28.4

The binding sites of Chlorine atom in the Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase (pdb code 2d0k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase, PDB code: 2d0k:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1162 b:28.7 occ:1.00 O A:HOH1168 3.1 29.8 1.0 N A:GLY96 3.1 24.1 1.0 OG1 A:THR46 3.3 35.6 1.0 N A:THR46 3.4 31.0 1.0 CA A:GLY43 3.4 20.2 1.0 C A:GLY43 3.5 21.0 1.0 N A:HIS45 3.6 30.9 1.0 CB A:HIS45 3.6 34.7 1.0 N A:GLY43 3.7 20.5 1.0 O A:GLY43 3.7 19.7 1.0 O A:HOH1214 3.8 54.7 1.0 CA A:HIS45 3.9 32.0 1.0 CA A:GLY96 3.9 21.8 1.0 C A:GLY95 4.0 21.4 1.0 ND1 A:HIS45 4.0 43.5 1.0 N A:ARG44 4.0 24.7 1.0 C A:HIS45 4.1 30.8 1.0 O A:GLY95 4.1 22.5 1.0 CB A:THR46 4.1 35.9 1.0 CA A:THR46 4.3 33.0 1.0 CG A:HIS45 4.3 41.6 1.0 CG2 A:VAL99 4.4 18.7 1.0 O A:HOH1196 4.5 43.2 1.0 C A:ARG44 4.5 29.5 1.0 O A:HOH1231 4.6 41.1 1.0 CA A:ARG44 4.9 27.5 1.0 C A:GLY96 4.9 22.6 1.0

Chlorine binding site 2 out of 2 in the Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl2162 b:37.9 occ:1.00 O B:HOH2178 3.1 69.0 1.0 OG1 B:THR46 3.2 27.1 1.0 N B:GLY96 3.2 25.6 1.0 N B:THR46 3.5 27.4 1.0 CA B:GLY43 3.5 22.4 1.0 N B:HIS45 3.6 30.2 1.0 C B:GLY43 3.6 25.8 1.0 CB B:HIS45 3.6 37.6 1.0 N B:GLY43 3.9 23.1 1.0 O B:GLY43 3.9 24.5 1.0 CA B:GLY96 3.9 23.7 1.0 CA B:HIS45 4.0 28.9 1.0 N B:ARG44 4.0 28.6 1.0 CB B:THR46 4.1 25.8 1.0 O B:HOH2252 4.2 61.0 1.0 C B:GLY95 4.2 23.8 1.0 C B:HIS45 4.2 28.4 1.0 O B:GLY95 4.3 24.1 1.0 ND1 B:HIS45 4.4 46.9 1.0 CA B:THR46 4.4 28.0 1.0 CG B:HIS45 4.4 43.7 1.0 CG2 B:VAL99 4.5 20.4 1.0 C B:ARG44 4.6 31.8 1.0 CA B:ARG44 4.9 32.1 1.0 C B:GLY96 4.9 23.9 1.0

M.Iwakura, K.Maki, H.Takahashi, T.Takenawa, A.Yokota, K.Katayanagi, T.Kamiyama, K.Gekko. Evolutional Design of A Hyperactive Cysteine- and Methionine-Free Mutant of Escherichia Coli Dihydrofolate Reductase J.Biol.Chem. V. 281 13234 2006.
ISSN: ISSN 0021-9258
PubMed: 16510443
DOI: 10.1074/JBC.M508823200