Chlorine 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:

Magnesium

(Mg)

4 atoms

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine 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 Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 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 Chlorine with other atoms in the Cl 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:Cl1602 b:63.9 occ:1.00 N A:LYS1334 3.3 46.7 1.0 CB A:LYS1334 3.4 38.4 1.0 C A:PRO1332 3.5 56.4 1.0 CA A:PRO1332 3.6 47.8 1.0 N A:LEU1333 3.7 46.5 1.0 CA A:MET1331 3.7 50.2 1.0 CG A:LYS1334 3.9 40.2 1.0 CA A:LYS1334 3.9 41.6 1.0 O A:PRO1332 4.0 52.4 1.0 CG A:MET1331 4.0 60.8 1.0 CB A:MET1331 4.2 55.7 1.0 CD A:LYS1334 4.3 39.6 1.0 N A:MET1331 4.4 49.5 1.0 C A:LEU1333 4.4 43.5 1.0 O A:HOH1795 4.5 44.1 1.0 CA A:LEU1333 4.6 46.7 1.0 N A:PRO1332 4.6 51.8 1.0 O A:THR1330 4.6 45.1 1.0 N A:LEU1335 4.7 42.0 1.0 C A:MET1331 4.7 60.2 1.0 C A:THR1330 4.7 47.3 1.0 CB A:PRO1332 4.7 47.9 1.0 C A:LYS1334 4.8 46.2 1.0 SD A:MET1331 4.9 97.1 1.0

Chlorine binding site 2 out of 2 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 Chlorine with other atoms in the Cl 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 D:Cl1602 b:69.0 occ:1.00 CB D:LYS1334 3.4 51.9 1.0 N D:LYS1334 3.6 53.5 1.0 CA D:PRO1332 3.8 61.2 1.0 C D:PRO1332 3.8 65.0 1.0 CG D:LYS1334 3.9 46.6 1.0 CA D:MET1331 4.0 57.2 1.0 CG D:MET1331 4.0 67.9 1.0 N D:LEU1333 4.1 57.4 1.0 CA D:LYS1334 4.1 51.0 1.0 O D:PRO1332 4.2 61.9 1.0 CD D:LYS1334 4.3 51.9 1.0 CB D:MET1331 4.4 62.0 1.0 N D:LEU1335 4.6 52.2 1.0 C D:LEU1333 4.7 54.4 1.0 N D:MET1331 4.7 63.2 1.0 CB D:PRO1332 4.7 60.2 1.0 C D:LYS1334 4.8 52.0 1.0 N D:PRO1332 4.8 62.1 1.0 O D:THR1330 4.9 53.5 1.0 CA D:LEU1333 4.9 52.1 1.0 SD D:MET1331 4.9 92.5 1.0 C D:MET1331 5.0 60.7 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