Chlorine in PDB 5j8z: Human Carbonic Anhydrase II in Complex with Ligand

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with Ligand:
4.2.1.1;

The structure of Human Carbonic Anhydrase II in Complex with Ligand, PDB code: 5j8z was solved by V.Alterio, G.De Simone, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.396, 41.390, 71.823, 90.00, 104.24, 90.00
R / Rfree (%)	16.2 / 19.5

The structure of Human Carbonic Anhydrase II in Complex with Ligand also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Human Carbonic Anhydrase II in Complex with Ligand (pdb code 5j8z). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Carbonic Anhydrase II in Complex with Ligand, PDB code: 5j8z:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Carbonic Anhydrase II in Complex with Ligand


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Carbonic Anhydrase II in Complex with Ligand within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl303 b:38.1 occ:0.50 CL A:FC4303 0.0 38.1 0.5 CL A:6KE304 0.7 35.6 0.5 C18 A:FC4303 1.7 38.0 0.5 C18 A:6KE304 1.9 37.7 0.5 C19 A:6KE304 2.5 37.8 0.5 C19 A:FC4303 2.7 37.5 0.5 C17 A:FC4303 2.7 37.3 0.5 C17 A:6KE304 3.1 37.3 0.5 O A:HOH615 3.7 26.2 1.0 C20 A:6KE304 3.8 37.8 0.5 C20 A:FC4303 4.0 36.1 0.5 C16 A:FC4303 4.0 36.0 0.5 O A:HOH497 4.1 24.6 1.0 C16 A:6KE304 4.3 37.5 0.5 CD1 A:ILE91 4.3 10.1 1.0 C15 A:FC4303 4.5 34.4 0.5 C15 A:6KE304 4.6 37.1 0.5 CG1 A:ILE91 5.0 7.3 1.0

Chlorine binding site 2 out of 2 in the Human Carbonic Anhydrase II in Complex with Ligand


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Carbonic Anhydrase II in Complex with Ligand within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl304 b:35.6 occ:0.50 CL A:6KE304 0.0 35.6 0.5 CL A:FC4303 0.7 38.1 0.5 C18 A:6KE304 1.7 37.7 0.5 C18 A:FC4303 1.8 38.0 0.5 C17 A:FC4303 2.4 37.3 0.5 C19 A:6KE304 2.7 37.8 0.5 C17 A:6KE304 2.7 37.3 0.5 C19 A:FC4303 3.0 37.5 0.5 C16 A:FC4303 3.7 36.0 0.5 CD1 A:ILE91 4.0 10.1 1.0 C20 A:6KE304 4.0 37.8 0.5 C16 A:6KE304 4.0 37.5 0.5 O A:HOH615 4.1 26.2 1.0 C20 A:FC4303 4.2 36.1 0.5 O A:HOH497 4.3 24.6 1.0 C15 A:FC4303 4.5 34.4 0.5 C15 A:6KE304 4.5 37.1 0.5 CG1 A:ILE91 4.7 7.3 1.0

D.Vullo, C.T.Supuran, A.Scozzafava, G.De Simone, S.M.Monti, V.Alterio, F.Carta. Kinetic and X-Ray Crystallographic Investigations of Substituted 2-Thio-6-Oxo-1, 6-Dihydropyrimidine-Benzenesulfonamides Acting As Carbonic Anhydrase Inhibitors. Bioorg.Med.Chem. V. 24 3643 2016.
ISSN: ESSN 1464-3391
PubMed: 27316543
DOI: 10.1016/J.BMC.2016.06.005