Chlorine in PDB 8rs5: Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4

All present enzymatic activity of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4:
1.1.1.299;

The structure of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4, PDB code: 8rs5 was solved by S.Coquille, S.Engilberge, D.Madern, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.92 / 1.95
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	74.36, 74.36, 267.67, 90, 90, 90
R / Rfree (%)	25.8 / 28.3

The structure of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4 also contains other interesting chemical elements:

Potassium

(K)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4 (pdb code 8rs5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4, PDB code: 8rs5:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:26.9 occ:1.00 HE A:ARG20 2.4 29.4 1.0 HE B:ARG20 2.4 27.7 1.0 HH21 B:ARG20 2.7 33.7 1.0 HG23 A:THR16 2.8 32.8 1.0 HH21 A:ARG20 2.9 25.7 1.0 HG23 B:THR16 2.9 31.1 1.0 HE1 B:PHE230 3.0 31.8 1.0 HE1 A:PHE230 3.2 31.0 1.0 HD1 B:PHE230 3.2 34.0 1.0 NE B:ARG20 3.3 23.0 1.0 NE A:ARG20 3.3 24.4 1.0 HD1 A:PHE230 3.3 33.7 1.0 HG22 A:THR16 3.4 32.8 1.0 CG2 A:THR16 3.4 27.3 1.0 NH2 B:ARG20 3.4 28.0 1.0 HG21 A:THR16 3.6 32.8 1.0 NH2 A:ARG20 3.6 21.4 1.0 CE1 B:PHE230 3.7 26.4 1.0 CG2 B:THR16 3.7 25.8 1.0 HG3 A:ARG20 3.8 27.5 1.0 CD1 B:PHE230 3.8 28.3 1.0 CZ B:ARG20 3.8 24.6 1.0 HG2 A:ARG20 3.8 27.5 1.0 HG22 B:THR16 3.8 31.1 1.0 CE1 A:PHE230 3.8 25.8 1.0 HG21 B:THR16 3.9 31.1 1.0 CD1 A:PHE230 3.9 28.1 1.0 CZ A:ARG20 3.9 26.0 1.0 HG2 B:ARG20 3.9 31.5 1.0 HG3 B:ARG20 4.0 31.5 1.0 CG A:ARG20 4.1 22.9 1.0 HH22 B:ARG20 4.2 33.7 1.0 CG B:ARG20 4.3 26.2 1.0 CD A:ARG20 4.3 27.5 1.0 HH22 A:ARG20 4.3 25.7 1.0 CD B:ARG20 4.4 22.9 1.0 HB3 A:ALA19 4.4 29.8 1.0 O B:HOH602 4.4 28.3 1.0 HB3 B:ALA19 4.5 27.5 1.0 HA A:THR16 4.5 29.2 1.0 HA B:THR16 4.6 32.4 1.0 HD2 A:ARG20 4.8 33.1 1.0 CB A:THR16 4.8 27.1 1.0 HD2 B:ARG20 4.8 27.6 1.0 HB1 A:ALA19 4.9 29.8 1.0 O A:THR16 4.9 23.7 1.0 CB B:THR16 4.9 25.4 1.0 CZ B:PHE230 4.9 29.0 1.0 HB1 B:ALA19 5.0 27.5 1.0 HD3 A:ARG20 5.0 33.1 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl403 b:37.6 occ:1.00 H A:THR252 2.4 35.1 1.0 O A:HOH504 2.8 39.2 1.0 HB2 A:SER152 2.9 38.1 1.0 HB A:THR252 3.1 38.2 1.0 N A:THR252 3.2 29.2 1.0 HA A:LEU251 3.2 36.0 1.0 ND1 A:HIS149 3.3 25.2 1.0 HA A:HIS149 3.4 35.4 1.0 OG1 A:THR252 3.4 30.5 1.0 HB3 A:SER152 3.5 38.1 1.0 CB A:THR252 3.6 31.8 1.0 CB A:SER152 3.6 31.7 1.0 HG A:SER152 3.6 39.6 1.0 HG1 A:THR252 3.7 36.6 1.0 HE1 A:HIS149 3.9 34.8 1.0 HD22 A:LEU251 3.9 38.1 1.0 CA A:THR252 4.0 29.1 1.0 HH12 A:ARG173 4.0 46.5 1.0 CE1 A:HIS149 4.0 29.0 1.0 HB3 A:LEU251 4.0 35.0 1.0 CA A:LEU251 4.0 29.9 1.0 HG3 A:MET153 4.0 35.5 0.5 O A:HIS149 4.0 29.3 1.0 C A:LEU251 4.1 31.8 1.0 OG A:SER152 4.1 33.0 1.0 HG2 A:MET153 4.1 35.5 0.5 CA A:HIS149 4.3 29.4 1.0 HD23 A:LEU251 4.4 38.1 1.0 CG A:HIS149 4.5 25.8 1.0 NH1 A:ARG173 4.5 38.7 1.0 O A:THR252 4.5 32.8 1.0 SD A:MET153 4.5 31.2 0.5 CB A:LEU251 4.5 29.1 1.0 HH11 A:ARG173 4.6 46.5 1.0 CD2 A:LEU251 4.6 31.7 1.0 C A:HIS149 4.6 27.6 1.0 HB3 A:ARG173 4.6 44.9 1.0 C A:THR252 4.7 30.2 1.0 O A:VAL250 4.7 27.8 1.0 HA A:THR252 4.8 34.9 1.0 CB A:HIS149 4.8 30.1 1.0 CG A:MET153 4.8 29.5 0.5 HB2 A:HIS149 4.9 36.2 1.0 CG A:MET153 4.9 29.5 0.5 HG2 A:MET153 4.9 35.5 0.5 HA A:ARG173 4.9 40.2 1.0 CA A:SER152 4.9 29.4 1.0 O A:THR172 4.9 34.5 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl402 b:30.9 occ:1.00 HD1 B:HIS149 2.5 31.1 1.0 H B:THR252 2.5 30.0 1.0 HB2 B:SER152 2.9 34.2 1.0 HA B:LEU251 3.2 33.3 1.0 ND1 B:HIS149 3.3 25.8 1.0 N B:THR252 3.3 25.0 1.0 HB3 B:SER152 3.4 34.2 1.0 HB B:THR252 3.4 36.9 1.0 HA B:HIS149 3.5 34.7 1.0 CB B:SER152 3.6 28.4 1.0 OG1 B:THR252 3.7 28.8 1.0 HE1 B:HIS149 3.7 34.7 1.0 HD22 B:LEU251 3.7 33.4 1.0 HB3 B:LEU251 3.7 31.0 1.0 HG B:SER152 3.8 36.3 1.0 HG3 B:MET153 3.8 34.6 0.5 CE1 B:HIS149 3.9 28.9 1.0 CB B:THR252 3.9 30.7 1.0 HG2 B:MET153 4.0 34.4 0.5 O B:HIS149 4.0 28.9 1.0 CA B:LEU251 4.0 27.7 1.0 HH12 B:ARG173 4.1 37.6 1.0 HD23 B:LEU251 4.1 33.4 1.0 OG B:SER152 4.2 30.2 1.0 C B:LEU251 4.2 25.8 1.0 CA B:THR252 4.2 27.4 1.0 HH11 B:ARG173 4.3 37.6 1.0 CB B:LEU251 4.3 25.8 1.0 CD2 B:LEU251 4.4 27.8 1.0 CA B:HIS149 4.4 28.8 1.0 NH1 B:ARG173 4.4 31.3 1.0 HG1 B:THR252 4.5 34.6 1.0 CG B:HIS149 4.5 26.9 1.0 SD B:MET153 4.6 29.1 0.5 HG2 B:MET153 4.6 34.6 0.5 O B:THR252 4.6 25.1 1.0 C B:HIS149 4.6 28.2 1.0 CG B:MET153 4.6 28.8 0.5 HG3 B:ARG173 4.7 42.1 1.0 CG B:MET153 4.7 28.6 0.5 O B:VAL250 4.8 29.2 1.0 CA B:SER152 4.9 31.0 1.0 CB B:HIS149 4.9 26.5 1.0 N B:MET153 4.9 28.1 1.0 C B:THR252 4.9 27.6 1.0 HA B:THR252 5.0 32.9 1.0 HB2 B:HIS149 5.0 31.9 1.0

S.Coquille, C.Simoes Pereira, C.Brochier-Armanet, J.Roche, G.Santoni, N.Coquelle, E.Girard, F.Sterpone, D.Madern. Navigating the Conformational Landscape of An Enzyme. Stabilization of A Low Populated Conformer By Evolutionary Mutations Triggers Allostery Into A Non-Allosteric Enzyme. To Be Published.