Chlorine in PDB 2x5k: Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli

All present enzymatic activity of Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli:
1.2.1.72;

The structure of Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli, PDB code: 2x5k was solved by S.Moniot, C.Didierjean, S.Boschi-Muller, G.Branlant, C.Corbier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.97 / 2.37
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	134.810, 134.810, 246.110, 90.00, 90.00, 90.00
R / Rfree (%)	16.444 / 20.699

The binding sites of Chlorine atom in the Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli (pdb code 2x5k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli, PDB code: 2x5k:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ O:Cl1339 b:47.1 occ:1.00 OG1 O:THR48 2.9 32.4 1.0 NE R:ARG197 3.3 23.0 1.0 CB O:THR48 3.4 32.5 1.0 N R:ALA198 3.5 34.3 1.0 N O:THR48 3.6 30.7 1.0 CA R:ARG197 3.7 36.3 1.0 O O:HOH2003 3.8 44.8 1.0 NH1 O:ARG10 3.8 19.1 1.0 CD R:ARG197 3.9 23.5 1.0 CA O:THR48 4.1 32.1 1.0 O R:THR196 4.1 40.2 1.0 C R:ARG197 4.1 35.2 1.0 CB R:ARG197 4.2 35.8 1.0 OD1 O:ASP47 4.3 31.8 1.0 CB R:ALA198 4.3 31.7 1.0 CZ R:ARG197 4.4 24.3 1.0 NH1 R:ARG197 4.4 16.8 1.0 CA R:ALA198 4.5 33.5 1.0 O O:HOH2032 4.6 25.5 1.0 CG2 O:THR48 4.7 30.6 1.0 C O:ASP47 4.7 29.3 1.0 CG R:ARG197 4.7 35.6 1.0 O R:HOH2138 4.8 26.4 1.0 N R:ARG197 4.8 36.9 1.0 CZ O:ARG10 4.9 24.1 1.0 C R:THR196 4.9 39.8 1.0 CG O:ASP47 4.9 30.4 1.0 CA O:ASP47 4.9 28.0 1.0

Chlorine binding site 2 out of 3 in the Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ P:Cl1338 b:29.2 occ:1.00 OG1 P:THR48 2.7 19.6 1.0 CB P:THR48 3.3 22.9 1.0 O Q:HOH2163 3.3 41.6 1.0 NE Q:ARG197 3.4 23.7 1.0 N Q:ALA198 3.5 27.6 1.0 N P:THR48 3.5 24.2 1.0 CA Q:ARG197 3.7 27.9 1.0 NH2 P:ARG10 3.8 13.4 1.0 CE1 P:HIS180 3.9 39.3 1.0 O P:HOH2157 4.0 36.8 1.0 CA P:THR48 4.0 22.4 1.0 C Q:ARG197 4.1 28.0 1.0 NH1 Q:ARG197 4.1 17.9 1.0 CD Q:ARG197 4.1 23.6 1.0 OD1 P:ASP47 4.2 36.2 1.0 CB Q:ARG197 4.2 27.3 1.0 CZ Q:ARG197 4.2 27.1 1.0 CB Q:ALA198 4.3 27.8 1.0 ND1 P:HIS180 4.4 40.0 1.0 O Q:THR196 4.4 31.5 1.0 C P:ASP47 4.5 25.0 1.0 CA Q:ALA198 4.5 27.5 1.0 CA P:ASP47 4.6 26.3 1.0 CG2 P:THR48 4.7 18.7 1.0 O P:HOH2010 4.7 27.7 1.0 N Q:ARG197 4.8 28.5 1.0 CG P:ASP47 4.8 29.5 1.0 CG Q:ARG197 4.8 27.9 1.0 O Q:HOH2165 4.9 27.6 1.0 CZ P:ARG10 4.9 15.9 1.0 C Q:THR196 5.0 29.4 1.0

Chlorine binding site 3 out of 3 in the Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of An Active Site Mutant of the D-Erythrose-4-Phosphate Dehydrogenase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ Q:Cl1339 b:38.0 occ:1.00 OG1 Q:THR48 2.9 24.8 1.0 N P:ALA198 3.3 28.9 1.0 CB Q:THR48 3.3 25.5 1.0 O Q:HOH2145 3.4 56.6 1.0 NE P:ARG197 3.6 26.7 1.0 N Q:THR48 3.7 26.8 1.0 CA P:ARG197 3.7 29.9 1.0 CB P:ALA198 4.0 28.4 1.0 C P:ARG197 4.0 30.0 1.0 CB P:ARG197 4.1 28.4 1.0 CA Q:THR48 4.1 27.0 1.0 O P:HOH2160 4.2 42.9 1.0 NH2 Q:ARG10 4.2 18.8 1.0 CA P:ALA198 4.2 28.9 1.0 OD2 Q:ASP47 4.3 35.1 1.0 CD P:ARG197 4.3 21.9 1.0 O P:THR196 4.3 33.8 1.0 NH1 P:ARG197 4.4 19.0 1.0 CZ P:ARG197 4.5 24.2 1.0 CG2 Q:THR48 4.5 26.4 1.0 O P:HOH2177 4.7 17.6 1.0 C Q:ASP47 4.8 28.5 1.0 CG P:ARG197 4.8 27.6 1.0 O Q:HOH2036 4.9 25.1 1.0 N P:ARG197 4.9 30.6 1.0

S.Moniot, C.Didierjean, S.Boschi-Muller, G.Branlant, C.Corbier. Structural Characterization of Erythrose-4- Phosphate Dehydrogenase From Escherichia Coli: Peculiar Features When Compared to Phosphorylating Gapdhs To Be Published.