Potassium 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:

Chlorine

(Cl)

3 atoms

The binding sites of Potassium 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 Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4, PDB code: 8rs5:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in the Crystal Structure of Methanopyrus Kandleri Malate Dehydrogenase Mutant 4


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K 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:K404 b:30.5 occ:1.00 O A:LEU24 2.6 30.3 1.0 O A:ALA22 2.6 28.6 1.0 O A:VAL27 2.6 27.5 1.0 HB2 A:ALA60 2.7 39.9 1.0 O A:ASP59 2.8 35.8 1.0 O A:HOH595 2.8 30.8 1.0 O A:HOH545 2.9 35.4 1.0 C A:LEU24 3.6 30.1 1.0 HA A:ASP25 3.6 37.9 1.0 C A:ALA22 3.8 27.2 1.0 CB A:ALA60 3.8 33.2 1.0 O A:HOH556 3.8 36.9 1.0 C A:VAL27 3.8 29.4 1.0 C A:ASP59 3.9 38.0 1.0 HB A:VAL27 4.0 35.5 1.0 H A:VAL27 4.0 36.9 1.0 HA A:ASN28 4.1 38.6 1.0 HA A:ALA60 4.2 45.6 1.0 HB1 A:ALA60 4.2 39.9 1.0 N A:LEU24 4.2 27.9 1.0 C A:LEU23 4.2 29.2 1.0 H A:ASP59 4.2 43.5 1.0 HA A:ALA22 4.3 35.2 1.0 HB3 A:LYS58 4.3 39.9 1.0 CA A:ASP25 4.3 31.5 1.0 O A:HOH552 4.3 37.2 1.0 N A:ASP25 4.4 30.7 1.0 HA A:LEU23 4.4 31.0 1.0 H A:LEU24 4.4 33.5 1.0 CA A:ALA60 4.4 37.9 1.0 HB3 A:ALA60 4.4 39.9 1.0 O A:LEU23 4.5 30.8 1.0 N A:ALA60 4.5 38.8 1.0 CA A:LEU24 4.5 25.7 1.0 N A:VAL27 4.6 30.7 1.0 N A:LEU23 4.6 26.9 1.0 CA A:VAL27 4.6 30.0 1.0 CA A:ALA22 4.6 29.3 1.0 CA A:LEU23 4.6 25.8 1.0 HG12 A:VAL27 4.7 38.0 1.0 C A:ASP25 4.7 32.1 1.0 CB A:VAL27 4.7 29.6 1.0 O A:ASP25 4.8 30.6 1.0 N A:ASN28 4.8 28.8 1.0 N A:ASP59 4.9 36.2 1.0 CA A:ASN28 4.9 32.1 1.0 O A:LEU21 5.0 26.2 1.0 HD22 A:LEU53 5.0 39.3 1.0

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


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K 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 B:K403 b:28.1 occ:1.00 O B:VAL27 2.6 29.9 1.0 O B:LEU24 2.6 25.3 1.0 O B:ASP59 2.7 32.6 1.0 O B:HOH581 2.7 35.8 1.0 O B:ALA22 2.8 23.6 1.0 O B:HOH539 2.9 34.6 1.0 HB2 B:ALA60 2.9 39.1 1.0 C B:LEU24 3.6 26.6 1.0 HA B:ASP25 3.7 37.2 1.0 C B:VAL27 3.8 31.3 1.0 C B:ALA22 3.8 23.7 1.0 CB B:ALA60 3.8 32.5 1.0 C B:ASP59 3.9 36.7 1.0 HA B:ASN28 4.0 38.9 1.0 HB B:VAL27 4.1 31.7 1.0 H B:ASP59 4.1 45.3 1.0 HB1 B:ALA60 4.1 39.1 1.0 H B:VAL27 4.1 33.6 1.0 HA B:ALA60 4.2 41.1 1.0 C B:LEU23 4.2 27.1 1.0 N B:LEU24 4.2 28.1 1.0 HA B:ALA22 4.3 27.5 1.0 CA B:ASP25 4.3 30.9 1.0 HA B:LEU23 4.3 33.2 1.0 N B:ASP25 4.4 28.0 1.0 O B:LEU23 4.4 28.4 1.0 HB3 B:LYS58 4.4 42.1 1.0 H B:LEU24 4.4 33.8 1.0 CA B:ALA60 4.4 34.2 1.0 HB3 B:ALA60 4.4 39.1 1.0 CA B:LEU24 4.5 29.0 1.0 O B:HOH568 4.6 40.3 1.0 N B:ALA60 4.6 35.3 1.0 O B:ASP25 4.6 28.5 1.0 C B:ASP25 4.6 29.9 1.0 CA B:LEU23 4.6 27.6 1.0 CA B:VAL27 4.6 27.1 1.0 N B:LEU23 4.7 24.1 1.0 N B:VAL27 4.7 27.9 1.0 CA B:ALA22 4.7 22.9 1.0 N B:ASN28 4.7 30.6 1.0 N B:ASP59 4.7 37.7 1.0 CA B:ASN28 4.7 32.4 1.0 CB B:VAL27 4.8 26.3 1.0 HD22 B:LEU53 4.8 34.5 1.0 HG12 B:VAL27 4.8 31.6 1.0 CA B:ASP59 4.9 38.3 1.0 O B:LEU21 5.0 22.2 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.