Chlorine in PDB 8rwl: Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 1

All present enzymatic activity of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 1:
1.1.1.299;

The structure of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 1, PDB code: 8rwl was solved by S.Coquille, J.Roche, S.Engilberge, E.Girard, D.Madern, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.92 / 2.30
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	78.25, 78.25, 251.3, 90, 90, 90
R / Rfree (%)	20.4 / 24.3

The structure of Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 1 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 1 (pdb code 8rwl). 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 1, PDB code: 8rwl:
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 1


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 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl404 b:57.2 occ:1.00 HE B:ARG20 2.3 53.5 1.0 HE A:ARG20 2.3 50.6 1.0 HH21 A:ARG20 2.6 49.1 1.0 HH21 B:ARG20 2.7 54.6 1.0 HG23 A:THR16 2.9 61.9 1.0 HG23 B:THR16 2.9 63.4 1.0 HE1 B:PHE230 3.1 49.0 1.0 HE1 A:PHE230 3.1 57.9 1.0 NE B:ARG20 3.1 44.4 1.0 NE A:ARG20 3.1 42.0 1.0 HD1 A:PHE230 3.2 55.4 1.0 HD1 B:PHE230 3.2 50.4 1.0 NH2 A:ARG20 3.4 40.8 1.0 NH2 B:ARG20 3.5 45.3 1.0 HG22 B:THR16 3.6 63.4 1.0 CG2 B:THR16 3.6 52.7 1.0 CG2 A:THR16 3.6 51.4 1.0 HG22 A:THR16 3.7 61.9 1.0 HG2 B:ARG20 3.7 46.4 1.0 HG3 B:ARG20 3.7 46.4 1.0 CZ A:ARG20 3.7 45.2 1.0 CE1 B:PHE230 3.7 40.7 1.0 CE1 A:PHE230 3.7 48.1 1.0 HG3 A:ARG20 3.7 55.6 1.0 HG2 A:ARG20 3.7 55.6 1.0 CZ B:ARG20 3.8 42.7 1.0 CD1 A:PHE230 3.8 46.0 1.0 CD1 B:PHE230 3.8 41.9 1.0 HG21 A:THR16 3.9 61.9 1.0 HG21 B:THR16 3.9 63.4 1.0 CG B:ARG20 4.0 38.5 1.0 CG A:ARG20 4.1 46.2 1.0 HH22 A:ARG20 4.1 49.1 1.0 CD B:ARG20 4.2 43.2 1.0 HH22 B:ARG20 4.2 54.6 1.0 CD A:ARG20 4.2 44.8 1.0 HB3 B:ALA19 4.4 49.5 1.0 HB3 A:ALA19 4.5 51.9 1.0 HA B:THR16 4.6 53.6 1.0 HA A:THR16 4.6 56.7 1.0 HD2 B:ARG20 4.7 52.1 1.0 HD2 A:ARG20 4.7 54.0 1.0 HD3 B:ARG20 4.8 52.1 1.0 CB A:THR16 4.9 50.5 1.0 HD3 A:ARG20 4.9 54.0 1.0 O B:THR16 4.9 39.6 1.0 CB B:THR16 4.9 42.2 1.0 O A:THR16 4.9 47.7 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 1


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 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl405 b:73.7 occ:1.00 HH12 A:ARG154 2.4 74.5 1.0 HE2 A:HIS178 2.7 100.4 1.0 H41N A:NDP401 2.9 71.8 1.0 HH22 A:ARG154 2.9 69.7 1.0 O A:HOH536 3.1 83.0 1.0 H72N A:NDP401 3.1 102.3 1.0 NH1 A:ARG154 3.2 61.9 1.0 HD23 A:LEU150 3.4 82.9 1.0 NE2 A:HIS178 3.4 83.5 1.0 HG A:SER228 3.5 77.0 1.0 HA3 A:GLY218 3.5 69.4 1.0 NH2 A:ARG154 3.6 57.9 1.0 HA2 A:GLY218 3.6 69.4 1.0 N7N A:NDP401 3.7 85.1 1.0 HD22 A:ASN123 3.7 80.8 1.0 C4N A:NDP401 3.8 59.7 1.0 HH11 A:ARG154 3.9 74.5 1.0 CZ A:ARG154 3.9 54.6 1.0 HE1 A:HIS178 3.9 96.0 1.0 CA A:GLY218 4.0 57.7 1.0 CE1 A:HIS178 4.0 79.9 1.0 C3N A:NDP401 4.1 67.1 1.0 H71N A:NDP401 4.1 102.3 1.0 OG A:SER228 4.1 64.0 1.0 CD2 A:LEU150 4.2 69.0 1.0 C7N A:NDP401 4.2 85.8 1.0 HH21 A:ARG154 4.3 69.7 1.0 HD21 A:LEU150 4.4 82.9 1.0 H42N A:NDP401 4.4 71.8 1.0 HD22 A:LEU150 4.5 82.9 1.0 ND2 A:ASN123 4.5 67.2 1.0 CD2 A:HIS178 4.6 69.3 1.0 HB3 A:SER228 4.6 64.2 1.0 HD21 A:ASN123 4.7 80.8 1.0 C5N A:NDP401 4.7 64.4 1.0 HD2 A:HIS178 4.8 83.4 1.0 C2N A:NDP401 4.8 64.0 1.0 O A:HOH514 4.8 61.6 1.0 H A:GLY218 4.9 81.9 1.0 N A:GLY218 4.9 68.1 1.0 CB A:SER228 5.0 53.3 1.0

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


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 1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl404 b:64.0 occ:1.00 HE2 B:HIS178 2.7 87.0 1.0 HH12 B:ARG154 2.9 85.5 1.0 HH22 B:ARG154 3.0 78.7 1.0 H41N B:NDP401 3.1 77.8 1.0 HG B:SER228 3.3 79.6 1.0 HD23 B:LEU150 3.4 92.7 1.0 NE2 B:HIS178 3.5 72.4 1.0 HD22 B:ASN123 3.6 82.2 1.0 NH1 B:ARG154 3.7 71.1 1.0 HA3 B:GLY218 3.8 87.6 1.0 NH2 B:ARG154 3.8 65.4 1.0 O7N B:NDP401 3.9 70.8 1.0 C4N B:NDP401 4.0 64.7 1.0 OG B:SER228 4.0 66.2 1.0 HA2 B:GLY218 4.0 87.6 1.0 HE1 B:HIS178 4.0 85.4 1.0 HD21 B:LEU150 4.0 92.7 1.0 C3N B:NDP401 4.1 66.4 1.0 CD2 B:LEU150 4.1 77.1 1.0 O B:HOH544 4.2 78.1 1.0 CE1 B:HIS178 4.2 71.0 1.0 CZ B:ARG154 4.3 64.1 1.0 ND2 B:ASN123 4.3 68.4 1.0 C7N B:NDP401 4.4 68.9 1.0 CA B:GLY218 4.4 72.9 1.0 HH11 B:ARG154 4.4 85.5 1.0 HB3 B:SER228 4.4 60.5 1.0 HD21 B:ASN123 4.4 82.2 1.0 HH21 B:ARG154 4.5 78.7 1.0 C5N B:NDP401 4.6 65.1 1.0 HD22 B:LEU150 4.6 92.7 1.0 CD2 B:HIS178 4.6 72.4 1.0 C2N B:NDP401 4.7 72.7 1.0 CB B:SER228 4.8 50.2 1.0 H42N B:NDP401 4.8 77.8 1.0 HD2 B:HIS178 4.8 87.1 1.0 H5N B:NDP401 4.8 78.3 1.0 O B:HOH553 4.8 76.1 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.