Magnesium in PDB 7tbv: Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans

The structure of Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans, PDB code: 7tbv was solved by P.J.Stogios, E.Evdokimova, K.Michalska, R.Di Leo, A.Savchenko, A.Joachimiak, K.J.F.Satchell, Center For Structural Genomics Ofinfectious Diseases (Csgid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.82 / 2.30
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	77.682, 89.239, 270.708, 90, 90.28, 90
R / Rfree (%)	17.8 / 22.6

The structure of Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans (pdb code 7tbv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans, PDB code: 7tbv:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1601 b:42.6 occ:1.00 O A:HOH2019 2.4 37.7 1.0 O A:LEU1171 2.4 39.8 1.0 O A:HOH1754 2.5 24.7 1.0 O A:HOH2095 2.5 30.8 1.0 O A:LYS1198 2.5 33.4 1.0 O A:GLY1169 2.5 44.4 1.0 C A:GLY1169 3.4 38.2 1.0 C A:LEU1171 3.6 40.7 1.0 C A:LYS1198 3.7 28.5 1.0 O A:HOH2002 3.8 30.9 1.0 ND2 A:ASN1200 3.9 34.1 1.0 N A:LEU1171 4.0 40.9 1.0 N A:LYS1198 4.0 24.2 1.0 C A:GLU1170 4.0 55.1 1.0 OD2 A:ASP1166 4.1 29.2 1.0 N A:GLU1170 4.2 34.0 1.0 CA A:GLY1169 4.2 36.2 1.0 CA A:GLU1170 4.3 52.1 1.0 CA A:LYS1198 4.3 30.4 1.0 CA A:LEU1171 4.4 37.1 1.0 OD2 A:ASP1204 4.5 36.4 1.0 O A:GLU1170 4.5 48.2 1.0 OD1 A:ASP1204 4.5 38.6 1.0 CG A:ASP1204 4.6 34.9 1.0 CB A:LYS1198 4.6 36.4 1.0 N A:LYS1172 4.6 38.3 1.0 N A:ALA1199 4.8 30.0 1.0 CA A:LYS1172 4.9 35.8 1.0 O A:HOH1821 4.9 54.8 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1601 b:51.0 occ:1.00 O B:LEU1171 2.0 37.2 1.0 O B:HOH1760 2.3 40.7 1.0 O B:HOH1820 2.5 40.1 1.0 O B:GLY1169 2.7 51.8 1.0 O B:HOH1723 2.7 35.2 1.0 O B:LYS1198 2.8 36.0 1.0 C B:LEU1171 3.2 45.9 1.0 O B:HOH1804 3.6 33.4 1.0 N B:LEU1171 3.6 39.9 1.0 C B:GLY1169 3.7 47.9 1.0 ND2 B:ASN1200 3.8 40.4 1.0 C B:GLU1170 3.9 48.9 1.0 CA B:LEU1171 4.0 42.7 1.0 C B:LYS1198 4.0 35.9 1.0 OD1 B:ASP1204 4.1 43.0 1.0 N B:LYS1172 4.2 42.0 1.0 CA B:GLU1170 4.3 54.6 1.0 OD2 B:ASP1166 4.3 36.5 1.0 N B:GLU1170 4.3 47.9 1.0 O B:GLU1170 4.4 50.4 1.0 OD2 B:ASP1204 4.4 35.1 1.0 CG B:ASP1204 4.4 36.4 1.0 N B:LYS1198 4.4 30.5 1.0 CA B:LYS1172 4.6 41.9 1.0 CA B:GLY1169 4.6 49.0 1.0 CB B:LEU1171 4.7 39.1 1.0 CA B:LYS1198 4.7 34.3 1.0 CB B:LYS1198 5.0 40.0 1.0 N B:ALA1199 5.0 32.6 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg1601 b:68.3 occ:1.00 O C:LEU1171 2.5 57.4 1.0 O C:LYS1198 2.6 50.7 1.0 O C:HOH1858 2.6 49.7 1.0 O C:HOH1782 2.7 48.4 1.0 O C:GLY1169 2.7 75.0 1.0 C C:LEU1171 3.7 60.0 1.0 C C:GLY1169 3.7 69.3 1.0 C C:LYS1198 3.8 46.7 1.0 ND2 C:ASN1200 3.8 54.5 1.0 N C:LEU1171 3.9 73.3 1.0 O C:HOH1763 4.0 43.1 1.0 N C:LYS1198 4.3 45.2 1.0 OD2 C:ASP1204 4.4 46.9 1.0 CA C:LEU1171 4.4 66.6 1.0 OD1 C:ASP1204 4.4 77.9 1.0 CA C:GLY1169 4.5 62.3 1.0 N C:GLU1170 4.5 68.9 1.0 CG C:ASP1204 4.5 59.0 1.0 C C:GLU1170 4.5 78.3 1.0 CA C:LYS1198 4.5 42.4 1.0 CA C:GLU1170 4.5 80.5 1.0 N C:LYS1172 4.7 59.0 1.0 OD2 C:ASP1166 4.7 54.1 1.0 CB C:LYS1198 4.8 45.9 1.0 N C:ALA1199 4.8 41.9 1.0 CA C:LYS1172 4.9 56.6 1.0 CA C:ALA1199 5.0 46.5 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Shikimate Kinase + 3-Dehydroquinate Dehydratase + 3-Dehydroshikimate Dehydrogenase Domains of ARO1 From Candida Albicans within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg1601 b:52.9 occ:1.00 O D:HOH2111 2.2 45.0 1.0 O D:HOH1724 2.6 58.7 1.0 O D:LEU1171 2.7 62.3 1.0 O D:HOH1806 2.8 29.5 1.0 O D:LYS1198 2.9 37.4 1.0 O D:GLY1169 3.2 65.3 1.0 C D:LEU1171 3.7 49.4 1.0 OD1 D:ASP1204 3.9 46.0 1.0 C D:GLY1169 3.9 56.9 1.0 O D:HOH2124 4.0 68.7 1.0 C D:LYS1198 4.1 38.1 1.0 CG D:ASP1204 4.2 42.8 1.0 OD2 D:ASP1204 4.2 42.8 1.0 N D:LEU1171 4.3 50.6 1.0 OD2 D:ASP1166 4.4 32.2 1.0 ND2 D:ASN1200 4.4 55.6 1.0 N D:LYS1172 4.4 44.4 1.0 CA D:LYS1172 4.5 45.5 1.0 N D:LYS1198 4.5 28.5 1.0 CA D:GLY1169 4.5 45.2 1.0 N D:GLU1170 4.5 48.2 1.0 C D:GLU1170 4.6 66.6 1.0 CA D:LEU1171 4.6 46.1 1.0 CA D:GLU1170 4.7 69.4 1.0 O D:HOH1877 4.8 33.9 1.0 CA D:LYS1198 4.9 36.5 1.0

P.J.Stogios, S.D.Liston, C.Semper, B.Quade, K.Michalska, E.Evdokimova, S.Ram, Z.Otwinowski, D.Borek, L.E.Cowen, A.Savchenko. Molecular Analysis and Essentiality of ARO1 Shikimate Biosynthesis Multi-Enzyme in Candida Albicans. Life Sci Alliance V. 5 2022.
ISSN: ESSN 2575-1077
PubMed: 35512834
DOI: 10.26508/LSA.202101358