Chlorine in PDB 9end: Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 3

The structure of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 3, PDB code: 9end was solved by S.Coquille, J.Roche, E.Girard, D.Madern, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.78 / 1.95
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	78.82, 78.82, 251.51, 90, 90, 90
R / Rfree (%)	19.5 / 23

The structure of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 3 also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 3 (pdb code 9end). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 3, PDB code: 9end:

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


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 3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:37.5 occ:1.00 HE B:ARG20 2.3 41.6 1.0 HE A:ARG20 2.3 43.0 1.0 HH21 A:ARG20 2.6 41.5 1.0 HH21 B:ARG20 2.7 41.6 1.0 HE1 B:PHE230 3.0 41.8 1.0 HE1 A:PHE230 3.0 39.0 1.0 HG22 B:THR16 3.1 47.1 1.0 HG23 A:THR16 3.1 45.0 1.0 NE B:ARG20 3.2 34.6 1.0 NE A:ARG20 3.2 35.8 1.0 HD1 B:PHE230 3.2 41.7 1.0 HD1 A:PHE230 3.3 40.1 1.0 NH2 A:ARG20 3.4 34.6 1.0 NH2 B:ARG20 3.4 34.6 1.0 CE1 B:PHE230 3.6 34.8 1.0 CE1 A:PHE230 3.7 32.5 1.0 CZ A:ARG20 3.7 36.0 1.0 CZ B:ARG20 3.8 33.6 1.0 CD1 B:PHE230 3.8 34.7 1.0 HG3 B:ARG20 3.8 37.3 1.0 HG22 A:THR16 3.8 45.0 1.0 HG3 A:ARG20 3.8 43.3 1.0 CD1 A:PHE230 3.8 33.3 1.0 CG2 A:THR16 3.8 37.4 1.0 CG2 B:THR16 3.9 39.2 1.0 HG21 B:THR16 3.9 47.1 1.0 HG2 A:ARG20 3.9 43.3 1.0 HG2 B:ARG20 3.9 37.3 1.0 HH22 A:ARG20 4.1 41.5 1.0 HG23 B:THR16 4.1 47.1 1.0 HG21 A:THR16 4.1 45.0 1.0 HH22 B:ARG20 4.1 41.6 1.0 CG A:ARG20 4.2 36.0 1.0 CG B:ARG20 4.2 31.0 1.0 CD B:ARG20 4.2 34.6 1.0 CD A:ARG20 4.3 36.9 1.0 HB1 A:ALA19 4.5 38.5 1.0 HB3 B:ALA19 4.6 36.0 1.0 HD2 B:ARG20 4.7 41.5 1.0 HA B:THR16 4.7 36.5 1.0 HD2 A:ARG20 4.7 44.3 1.0 HA A:THR16 4.7 37.9 1.0 CZ B:PHE230 4.9 35.4 1.0 HD3 B:ARG20 5.0 41.5 1.0 HD3 A:ARG20 5.0 44.3 1.0 CZ A:PHE230 5.0 35.3 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.